메뉴 건너뛰기




Volumn 1807, Issue 11, 2011, Pages 1398-1413

The cytochrome bd respiratory oxygen reductases

Author keywords

Bacterial physiology; Disease; Metabolism; Microbe; Molecular bioenergetics; Oxidoreduction

Indexed keywords

CARBON MONOXIDE; COPPER; CYANIDE; CYANIDE INSENSITIVE QUINOL OXIDASE; CYTOCHROME BD; HEME; HYDROGEN PEROXIDE; OXIDOREDUCTASE; PROTEIN SUBUNIT; PROTON; QUINONE DERIVATIVE; RESPIRATORY OXYGEN REDUCTASE; UNCLASSIFIED DRUG;

EID: 80052756459     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.06.016     Document Type: Review
Times cited : (396)

References (290)
  • 1
    • 10444234271 scopus 로고    scopus 로고
    • Cytochrome c oxidase, ligands and electrons
    • DOI 10.1016/j.jinorgbio.2004.10.011, PII S0162013404003162, Heme-Diatomic Interactions, Part 1
    • M. Brunori, A. Giuffrè, and P. Sarti Cytochrome c oxidase, ligands and electrons J. Inorg. Biochem. 99 2005 324 336 (Pubitemid 39642985)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 324-336
    • Brunori, M.1    Giuffre, A.2    Sarti, P.3
  • 2
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • DOI 10.1146/annurev.biochem.75.062003.101730
    • J.P. Hosler, S. Ferguson-Miller, and D.A. Mills Energy transduction: proton transfer through the respiratory complexes Annu. Rev. Biochem. 75 2006 165 187 (Pubitemid 44118030)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 3
    • 33749137961 scopus 로고    scopus 로고
    • Transmembrane proton translocation by cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2006.05.020, PII S0005272806001472
    • G. Branden, R.B. Gennis, and P. Brzezinski Transmembrane proton translocation by cytochrome c oxidase Biochim. Biophys. Acta 1757 2006 1052 1063 (Pubitemid 44467836)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1052-1063
    • Branden, G.1    Gennis, R.B.2    Brzezinski, P.3
  • 4
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • DOI 10.1016/j.bbabio.2007.06.008, PII S0005272807001533
    • M. Wikström, and M.I. Verkhovsky Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases Biochim. Biophys. Acta 1767 2007 1200 1214 (Pubitemid 47498307)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1200-1214
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 5
    • 36148938761 scopus 로고    scopus 로고
    • Molecular mechanism of proton translocation by cytochrome c oxidase
    • DOI 10.1089/ars.2007.1705
    • I. Belevich, and M.I. Verkhovsky Molecular mechanism of proton translocation by cytochrome c oxidase Antioxid. Redox Signal. 10 2008 1 29 (Pubitemid 350115984)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.1 , pp. 1-29
    • Belevich, I.1    Verkhovsky, M.I.2
  • 6
    • 66349104071 scopus 로고    scopus 로고
    • Electron transfer and energy transduction in the terminal part of the respiratory chain - Lessons from bacterial model systems
    • O.M. Richter, and B. Ludwig Electron transfer and energy transduction in the terminal part of the respiratory chain - lessons from bacterial model systems Biochim. Biophys. Acta 1787 2009 626 634
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 626-634
    • Richter, O.M.1    Ludwig, B.2
  • 7
    • 77953770537 scopus 로고    scopus 로고
    • Variable proton-pumping stoichiometry in structural variants of cytochrome c oxidase
    • P. Brzezinski, and A.L. Johansson Variable proton-pumping stoichiometry in structural variants of cytochrome c oxidase Biochim. Biophys. Acta 1797 2010 710 723
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 710-723
    • Brzezinski, P.1    Johansson, A.L.2
  • 8
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • DOI 10.1016/S0005-2728(01)00169-4, PII S0005272801001694
    • M.M. Pereira, M. Santana, and M. Teixeira A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta 1505 2001 185 208 (Pubitemid 32378771)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.2-3 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 9
    • 46349107814 scopus 로고    scopus 로고
    • Looking for the minimum common denominator in haem-copper oxygen reductases: Towards a unified catalytic mechanism
    • M.M. Pereira, F.L. Sousa, A.F. Verissimo, and M. Teixeira Looking for the minimum common denominator in haem-copper oxygen reductases: towards a unified catalytic mechanism Biochim. Biophys. Acta 1777 2008 929 934
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 929-934
    • Pereira, M.M.1    Sousa, F.L.2    Verissimo, A.F.3    Teixeira, M.4
  • 10
    • 70349493006 scopus 로고    scopus 로고
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping Proc. Natl. Acad. Sci. U.S.A. 106 2009 16169 16173
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16169-16173
    • Chang, H.Y.1    Hemp, J.2    Chen, Y.3    Fee, J.A.4    Gennis, R.B.5
  • 16
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans Nature 376 1995 660 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 18
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, and S. Iwata The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 21
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment
    • C. Ostermeier, A. Harrenga, U. Ermler, and H. Michel Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment Proc. Natl. Acad. Sci. U.S.A. 94 1997 10547 10553
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 23
    • 66349128958 scopus 로고    scopus 로고
    • High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: New insights into the active site and the proton transfer pathways
    • J. Koepke, E. Olkhova, H. Angerer, H. Muller, G. Peng, and H. Michel High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways Biochim. Biophys. Acta 1787 2009 635 645
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 635-645
    • Koepke, J.1    Olkhova, E.2    Angerer, H.3    Muller, H.4    Peng, G.5    Michel, H.6
  • 24
    • 70450277402 scopus 로고    scopus 로고
    • Towards a structural elucidation of the alternative oxidase in plants
    • M.S. Albury, C. Elliott, and A.L. Moore Towards a structural elucidation of the alternative oxidase in plants Physiol. Plant. 137 2009 316 327
    • (2009) Physiol. Plant. , vol.137 , pp. 316-327
    • Albury, M.S.1    Elliott, C.2    Moore, A.L.3
  • 26
    • 0021099774 scopus 로고
    • The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain
    • M.J. Miller, and R.B. Gennis The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain J. Biol. Chem. 258 1983 9159 9165
    • (1983) J. Biol. Chem. , vol.258 , pp. 9159-9165
    • Miller, M.J.1    Gennis, R.B.2
  • 27
    • 0021272743 scopus 로고
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems J. Biol. Chem. 259 1984 3375 3381 (Pubitemid 14130554)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.5 , pp. 3375-3381
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 28
    • 0023802457 scopus 로고
    • The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli
    • G.N. Green, H. Fang, R.-J. Lin, G. Newton, M. Mather, C.D. Georgiou, and R.B. Gennis The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli J. Biol. Chem. 263 1988 13138 13143
    • (1988) J. Biol. Chem. , vol.263 , pp. 13138-13143
    • Green, G.N.1    Fang, H.2    Lin, R.-J.3    Newton, G.4    Mather, M.5    Georgiou, C.D.6    Gennis, R.B.7
  • 30
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • B.L. Trumpower, and R.B. Gennis Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation Annu. Rev. Biochem. 63 1994 675 716 (Pubitemid 24218646)
    • (1994) Annual Review of Biochemistry , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 31
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • DOI 10.1016/S0005-2728(97)00046-7, PII S0005272897000467
    • S. Jünemann Cytochrome bd terminal oxidase Biochim. Biophys. Acta 1321 1997 107 127 (Pubitemid 27390501)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1321 , Issue.2 , pp. 107-127
    • Junemann, S.1
  • 32
    • 0030131933 scopus 로고    scopus 로고
    • Cytochrome bd: Structure and properties
    • (translated from Biokhimiya (in Russian) (1996), 61, 786-799)
    • V.B. Borisov Cytochrome bd: structure and properties Biochemistry (Moscow) 61 1996 565 574 (translated from Biokhimiya (in Russian) (1996), 61, 786-799)
    • (1996) Biochemistry (Moscow) , vol.61 , pp. 565-574
    • Borisov, V.B.1
  • 33
    • 0033734197 scopus 로고    scopus 로고
    • Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers
    • M. Tsubaki, H. Hori, and T. Mogi Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers J. Inorg. Biochem. 82 2000 19 25
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 19-25
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3
  • 34
    • 0023913519 scopus 로고
    • The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits
    • M.J. Miller, M. Hermodson, and R.B. Gennis The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits J. Biol. Chem. 263 1988 5235 5240
    • (1988) J. Biol. Chem. , vol.263 , pp. 5235-5240
    • Miller, M.J.1    Hermodson, M.2    Gennis, R.B.3
  • 36
    • 0028791167 scopus 로고
    • Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli
    • M. Tsubaki, H. Hori, T. Mogi, and Y. Anraku Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli J. Biol. Chem. 270 1995 28565 28569
    • (1995) J. Biol. Chem. , vol.270 , pp. 28565-28569
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3    Anraku, Y.4
  • 37
    • 0033547815 scopus 로고    scopus 로고
    • Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands
    • V. Borisov, A.M. Arutyunyan, J.P. Osborne, R.B. Gennis, and A.A. Konstantinov Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands Biochemistry 38 1999 740 750
    • (1999) Biochemistry , vol.38 , pp. 740-750
    • Borisov, V.1    Arutyunyan, A.M.2    Osborne, J.P.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 43
    • 77954761715 scopus 로고    scopus 로고
    • Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy
    • F. Rappaport, J. Zhang, M.H. Vos, R.B. Gennis, and V.B. Borisov Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy Biochim. Biophys. Acta 1797 2010 1657 1664
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1657-1664
    • Rappaport, F.1    Zhang, J.2    Vos, M.H.3    Gennis, R.B.4    Borisov, V.B.5
  • 44
    • 0022383731 scopus 로고
    • The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli
    • M.J. Miller, and R.B. Gennis The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli J. Biol. Chem. 260 1985 14003 14008 (Pubitemid 16194602)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.26 , pp. 14003-14008
    • Miller, M.J.1    Gennis, R.B.2
  • 47
    • 35349019174 scopus 로고    scopus 로고
    • Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement
    • DOI 10.1074/jbc.M705562200
    • I. Belevich, V.B. Borisov, and M.I. Verkhovsky Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement J. Biol. Chem. 282 2007 28514 28519 (Pubitemid 47606033)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.39 , pp. 28514-28519
    • Belevich, I.1    Borisov, V.B.2    Verkhovsky, M.I.3
  • 49
    • 0030974371 scopus 로고    scopus 로고
    • Formation of pH and potential gradients by the reconstituted Azotobacter vinelandii cytochrome bd respiratory protection oxidase
    • J.F. Kolonay Jr., and R.J. Maier Formation of pH and potential gradients by the reconstituted Azotobacter vinelandii cytochrome bd respiratory protection oxidase J. Bacteriol. 179 1997 3813 3817 (Pubitemid 27233031)
    • (1997) Journal of Bacteriology , vol.179 , Issue.11 , pp. 3813-3817
    • Kolonay Jr., J.F.1    Maier, R.J.2
  • 50
    • 0031559960 scopus 로고    scopus 로고
    • Generation of protonic potential by the bd-type quinol oxidase of Azotobacter vinelandii
    • DOI 10.1016/S0014-5793(97)01047-8, PII S0014579397010478
    • Y.V. Bertsova, A.V. Bogachev, and V.P. Skulachev Generation of protonic potential by the bd-type quinol oxidase of Azotobacter vinelandii FEBS Lett. 414 1997 369 372 (Pubitemid 27389397)
    • (1997) FEBS Letters , vol.414 , Issue.2 , pp. 369-372
    • Bertsova, Y.V.1    Bogachev, A.V.2    Skulachev, V.P.3
  • 51
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • W.J. Ingledew, and R.K. Poole The respiratory chains of Escherichia coli Microbiol. Rev. 48 1984 222 271 (Pubitemid 14035389)
    • (1984) Microbiological Reviews , vol.48 , Issue.3 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2
  • 52
    • 0033928977 scopus 로고    scopus 로고
    • Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation
    • R.K. Poole, and G.M. Cook Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation Adv. Microb. Physiol. 43 2000 165 224 (Pubitemid 30481125)
    • (2000) Advances in Microbial Physiology , vol.43 , pp. 165-224
    • Poole, R.K.1    Cook, G.M.2
  • 53
    • 77954758595 scopus 로고    scopus 로고
    • A. Böck, R.C.I. J.B. Kaper, P.D. Karp, F.C. Neidhardt, T. Nyström, J.M. Slauch, C.L. Squires, D. Ussery, ASM Press Washington, DC
    • V.B. Borisov, and M.I. Verkhovsky A. Böck, R.C.I. J.B. Kaper, P.D. Karp, F.C. Neidhardt, T. Nyström, J.M. Slauch, C.L. Squires, D. Ussery, EcoSal - Escherichia coli and Salmonella: Cellular and Molecular Biology 2009 ASM Press Washington, DC http://www.ecosal.org
    • (2009) EcoSal - Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Borisov, V.B.1    Verkhovsky, M.I.2
  • 59
    • 39849107313 scopus 로고    scopus 로고
    • Analysis of the respiratory chain in ethanologenic Zymomonas mobilis with a cyanide-resistant bd-type ubiquinol oxidase as the only terminal oxidase and its possible physiological roles
    • DOI 10.1159/000112598
    • K. Sootsuwan, N. Lertwattanasakul, P. Thanonkeo, K. Matsushita, and M. Yamada Analysis of the respiratory chain in Ethanologenic Zymomonas mobilis with a cyanide-resistant bd-type ubiquinol oxidase as the only terminal oxidase and its possible physiological roles J. Mol. Microbiol. Biotechnol. 14 2008 163 175 (Pubitemid 351317202)
    • (2008) Journal of Molecular Microbiology and Biotechnology , vol.14 , Issue.4 , pp. 163-175
    • Sootsuwan, K.1    Lertwattanasakul, N.2    Thanonkeo, P.3    Matsushita, K.4    Yamada, M.5
  • 60
    • 58449135158 scopus 로고    scopus 로고
    • The multiple evolutionary histories of dioxygen reductases: Implications for the origin and evolution of aerobic respiration
    • C. Brochier-Armanet, E. Talla, and S. Gribaldo The multiple evolutionary histories of dioxygen reductases: implications for the origin and evolution of aerobic respiration Mol. Biol. Evol. 26 2009 285 297
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 285-297
    • Brochier-Armanet, C.1    Talla, E.2    Gribaldo, S.3
  • 61
    • 0021251072 scopus 로고
    • Characterization of the cytochrome d terminal oxidase complex of Escherichia coli using polyclonal and monoclonal antibodies
    • R.G. Kranz, and R.B. Gennis Characterization of the cytochrome d terminal oxidase complex of Escherichia coli using polyclonal and monoclonal antibodies J. Biol. Chem. 259 1984 7998 8003 (Pubitemid 14081225)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.12 , pp. 7998-8003
    • Kranz, R.G.1    Gennis, R.B.2
  • 62
    • 0023929761 scopus 로고
    • Trypsin proteolysis of the cytochrome d complex of Escherichia coli selectively inhibits ubiquinol oxidase activity while not affecting N,N,N′,N′-tetramethyl-p-phenylenediamine oxidase activity
    • R.M. Lorence, K. Carter, R.B. Gennis, K. Matsushita, and H.R. Kaback Trypsin proteolysis of the cytochrome d complex of Escherichia coli selectively inhibits ubiquinol oxidase activity while not affecting N,N,N′,N′- tetramethyl-p-phenylenediamine oxidase activity J. Biol. Chem. 11 1988 5271 5276
    • (1988) J. Biol. Chem. , vol.11 , pp. 5271-5276
    • Lorence, R.M.1    Carter, K.2    Gennis, R.B.3    Matsushita, K.4    Kaback, H.R.5
  • 63
    • 0025259440 scopus 로고
    • Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize a functional domain
    • T.J. Dueweke, and R.B. Gennis Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize a functional domain J. Biol. Chem. 265 1990 4273 4277
    • (1990) J. Biol. Chem. , vol.265 , pp. 4273-4277
    • Dueweke, T.J.1    Gennis, R.B.2
  • 64
    • 0025881879 scopus 로고
    • Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localizes a quinol oxidase domain
    • T.J. Dueweke, and R.B. Gennis Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localizes a quinol oxidase domain Biochemistry 30 1991 3401 3406
    • (1991) Biochemistry , vol.30 , pp. 3401-3406
    • Dueweke, T.J.1    Gennis, R.B.2
  • 65
    • 33644848768 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli
    • DOI 10.1074/jbc.M508206200
    • Y. Matsumoto, M. Murai, D. Fujita, K. Sakamoto, H. Miyoshi, M. Yoshida, and T. Mogi Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli J. Biol. Chem. 281 2006 1905 1912 (Pubitemid 43845775)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 1905-1912
    • Matsumoto, Y.1    Murai, M.2    Fujita, D.3    Sakamoto, K.4    Miyoshi, H.5    Yoshida, M.6    Mogi, T.7
  • 66
    • 33746556970 scopus 로고    scopus 로고
    • Probing the ubiquinol-binding site in cytochrome bd by site-directed mutagenesis
    • DOI 10.1021/bi060192w
    • T. Mogi, S. Akimoto, S. Endou, T. Watanabe-Nakayama, E. Mizuochi-Asai, and H. Miyoshi Probing the ubiquinol-binding site in cytochrome bd by site-directed mutagenesis Biochemistry 45 2006 7924 7930 (Pubitemid 44185510)
    • (2006) Biochemistry , vol.45 , Issue.25 , pp. 7924-7930
    • Mogi, T.1    Akimoto, S.2    Endou, S.3    Watanabe-Nakayama, T.4    Mizuochi-Asai, E.5    Miyoshi, H.6
  • 67
    • 0033044722 scopus 로고    scopus 로고
    • Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunit I
    • DOI 10.1016/S0005-2728(98)00171-6, PII S0005272898001716
    • J.P. Osborne, and R.B. Gennis Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunits I Biochim. Biophys. Acta 1410 1999 32 50 (Pubitemid 29074428)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1410 , Issue.1 , pp. 32-50
    • Osborne, J.P.1    Gennis, R.B.2
  • 68
    • 0032961870 scopus 로고    scopus 로고
    • Gene structure and quinol oxidase activity of a cytochrome bd-type oxidase from Bacillus stearothermophilus
    • DOI 10.1016/S0005-2728(99)00012-2, PII S0005272899000122
    • J. Sakamoto, E. Koga, T. Mizuta, C. Sato, S. Noguchi, and N. Sone Gene structure and quinol oxidase activity of a cytochrome bd-type oxidase from Bacillus stearothermophilus Biochim. Biophys. Acta 1411 1999 147 158 (Pubitemid 29182805)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1411 , Issue.1 , pp. 147-158
    • Sakamoto, J.1    Koga, E.2    Mizuta, T.3    Sato, C.4    Noguchi, S.5    Sone, N.6
  • 69
    • 0034047835 scopus 로고    scopus 로고
    • Menaquinol oxidase activity and primary structure of cytochrome bd from the amino-acid fermenting bacterium Corynebacterium glutamicum
    • DOI 10.1007/s002030000161
    • K. Kusumoto, M. Sakiyama, J. Sakamoto, S. Noguchi, and N. Sone Menaquinol oxidase activity and primary structure of cytochrome bd from the amino-acid fermenting bacterium Corynebacterium glutamicum Arch. Microbiol. 173 2000 390 397 (Pubitemid 30407477)
    • (2000) Archives of Microbiology , vol.173 , Issue.5-6 , pp. 390-397
    • Kusumoto, K.1    Sakiyama, M.2    Sakamoto, J.3    Noguchi, S.4    Sone, N.5
  • 71
    • 0028854401 scopus 로고
    • Isolation and characterization of mutants defective in the cyanide-insensitive respiratory pathway of Pseudomonas aeruginosa
    • L. Cunningham, and H.D. Williams Isolation and characterization of mutants defective in the cyanide-insensitive respiratory pathway of Pseudomonas aeruginosa J. Bacteriol. 177 1995 432 438
    • (1995) J. Bacteriol. , vol.177 , pp. 432-438
    • Cunningham, L.1    Williams, H.D.2
  • 73
    • 0030915436 scopus 로고    scopus 로고
    • The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide- insensitive terminal oxidase related to the cytochrome bd quinol oxidases
    • L. Cunningham, M. Pitt, and H.D. Williams The cioAB genes from Pseudomonas aeruginosa code for a novel cyanide-insensitive terminal oxidase related to the cytochrome bd quinol oxidases Mol. Microbiol. 24 1997 579 591 (Pubitemid 27241705)
    • (1997) Molecular Microbiology , vol.24 , Issue.3 , pp. 579-591
    • Cunningham, L.1    Pitt, M.2    Williams, H.D.3
  • 74
    • 34548218698 scopus 로고    scopus 로고
    • Essential role of cytochrome bd-related oxidase in cyanide resistance of Pseudomonas pseudoalcaligenes CECT5344
    • DOI 10.1128/AEM.00503-07
    • A. Quesada, M.I. Guijo, F. Merchan, B. Blazquez, M.I. Igeno, and R. Blasco Essential role of cytochrome bd-related oxidase in cyanide resistance of Pseudomonas pseudoalcaligenes CECT5344 Appl. Environ. Microbiol. 73 2007 5118 5124 (Pubitemid 47326641)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.16 , pp. 5118-5124
    • Quesada, A.1    Guijo, M.I.2    Merchan, F.3    Blazquez, B.4    Igeno, M.I.5    Blasco, R.6
  • 75
    • 33947366478 scopus 로고    scopus 로고
    • Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: The cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type
    • DOI 10.1128/JB.00897-06
    • R.J. Jackson, K.T. Elvers, L.J. Lee, M.D. Gidley, L.M. Wainwright, J. Lightfoot, S.F. Park, and R.K. Poole Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: the cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type J. Bacteriol. 189 2007 1604 1615 (Pubitemid 46446122)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1604-1615
    • Jackson, R.J.1    Elvers, K.T.2    Lee, L.J.3    Gidley, M.D.4    Wainwright, L.M.5    Lightfoot, J.6    Park, S.F.7    Poole, R.K.8
  • 76
    • 0020743150 scopus 로고
    • Membrane-bound respiratory chain of Pseudomonas aeruginosa grown aerobically. A KCN-insensitive alternate oxidase chain and its energetics
    • K. Matsushita, M. Yamada, E. Shinagawa, O. Adachi, and M. Ameyama Membrane-bound respiratory chain of Pseudomonas aeruginosa grown aerobically. A KCN-insensitive alternate oxidase chain and its energetics J. Biochem. 93 1983 1137 1144
    • (1983) J. Biochem. , vol.93 , pp. 1137-1144
    • Matsushita, K.1    Yamada, M.2    Shinagawa, E.3    Adachi, O.4    Ameyama, M.5
  • 77
    • 33748313067 scopus 로고    scopus 로고
    • Inactivation of the Pseudomonas putida cytochrome o ubiquinol oxidase leads to a significant change in the transcriptome and to increased expression of the CIO and cbb3-1 terminal oxidases
    • DOI 10.1111/j.1462-2920.2006.01061.x
    • G. Morales, A. Ugidos, and F. Rojo Inactivation of the Pseudomonas putida cytochrome o ubiquinol oxidase leads to a significant change in the transcriptome and to increased expression of the CIO and cbb3-1 terminal oxidases Environ. Microbiol. 8 2006 1764 1774 (Pubitemid 44326468)
    • (2006) Environmental Microbiology , vol.8 , Issue.10 , pp. 1764-1774
    • Morales, G.1    Ugidos, A.2    Rojo, F.3
  • 78
    • 33751585830 scopus 로고    scopus 로고
    • Microevolution of cytochrome bd oxidase in staphylococci and its implication in resistance to respiratory toxins released by Pseudomonas
    • DOI 10.1128/JB.00858-06
    • L. Voggu, S. Schlag, R. Biswas, R. Rosenstein, C. Rausch, and F. Gotz Microevolution of cytochrome bd oxidase in Staphylococci and its implication in resistance to respiratory toxins released by Pseudomonas J. Bacteriol. 188 2006 8079 8086 (Pubitemid 44845677)
    • (2006) Journal of Bacteriology , vol.188 , Issue.23 , pp. 8079-8086
    • Voggu, L.1    Schlag, S.2    Biswas, R.3    Rosenstein, R.4    Rausch, C.5    Gotz, F.6
  • 80
    • 66549099042 scopus 로고    scopus 로고
    • Properties of cytochrome bd plastoquinol oxidase from the cyanobacterium Synechocystis sp. PCC 6803
    • T. Mogi, and H. Miyoshi Properties of cytochrome bd plastoquinol oxidase from the cyanobacterium Synechocystis sp. PCC 6803 J. Biochem. 145 2009 395 401
    • (2009) J. Biochem. , vol.145 , pp. 395-401
    • Mogi, T.1    Miyoshi, H.2
  • 81
    • 0034099024 scopus 로고    scopus 로고
    • Mechanism, regulation, and ecological role of bacterial cyanide biosynthesis
    • DOI 10.1007/s002039900127
    • C. Blumer, and D. Haas Mechanism, regulation, and ecological role of bacterial cyanide biosynthesis Arch. Microbiol. 173 2000 170 177 (Pubitemid 30143574)
    • (2000) Archives of Microbiology , vol.173 , Issue.3 , pp. 170-177
    • Blumer, C.1    Haas, D.2
  • 82
    • 0021012711 scopus 로고
    • Hydrogen cyanide production by Pseudomonas aeruginosa at reduced oxygen levels
    • P.A. Castric Hydrogen cyanide production by Pseudomonas aeruginosa at reduced oxygen levels Can. J. Microbiol. 29 1983 1344 1349 (Pubitemid 14191527)
    • (1983) Canadian Journal of Microbiology , vol.29 , Issue.10 , pp. 1344-1349
    • Castric, P.A.1
  • 83
    • 0014045168 scopus 로고
    • Cyanide production by Pseudomonas aeruginosa
    • W.B. Goldfarb, and H. Margraf Cyanide production by Pseudomonas aeruginosa Ann. Surg. 165 1967 104 110
    • (1967) Ann. Surg. , vol.165 , pp. 104-110
    • Goldfarb, W.B.1    Margraf, H.2
  • 84
    • 33646797416 scopus 로고    scopus 로고
    • Investigation of the physiological relationship between the cyanide-insensitive oxidase and cyanide production in Pseudomonas aeruginosa
    • J.E.A. Zlosnik, G.R. Tavankar, J.G. Bundy, D. Mossialos, R. O'Toole, and H.D. Williams Investigation of the physiological relationship between the cyanide-insensitive oxidase and cyanide production in Pseudomonas aeruginosa Microbiology 152 2006 1407 1415
    • (2006) Microbiology , vol.152 , pp. 1407-1415
    • Zlosnik, J.E.A.1    Tavankar, G.R.2    Bundy, J.G.3    Mossialos, D.4    O'Toole, R.5    Williams, H.D.6
  • 85
    • 0038323991 scopus 로고    scopus 로고
    • Mutation or overexpression of a terminal oxidase leads to a cell division defect and multiple antibiotic sensitivity in Pseudomonas aeruginosa
    • DOI 10.1074/jbc.M210355200
    • G.R. Tavankar, D. Mossialos, and H.D. Williams Mutation or overexpression of a terminal oxidase leads to a cell division defect and multiple antibiotic sensitivity in Pseudomonas aeruginosa J. Biol. Chem. 278 2003 4524 4530 (Pubitemid 36800948)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4524-4530
    • Tavankar, G.R.1    Mossialos, D.2    Williams, H.D.3
  • 86
    • 0842264185 scopus 로고    scopus 로고
    • The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen
    • DOI 10.1038/nature02285
    • A.D. Baughn, and M.H. Malamy The strict anaerobe Bacteroides fragilis grows in and benefits from nanomolar concentrations of oxygen Nature 427 2004 441 444 (Pubitemid 38168496)
    • (2004) Nature , vol.427 , Issue.6973 , pp. 441-444
    • Baughn, A.D.1    Malamy, M.H.2
  • 88
    • 27744527534 scopus 로고    scopus 로고
    • Differential use of the two high-oxygen-affinity terminal oxidases of Brucella suis for in vitro and intramacrophagic multiplication
    • DOI 10.1128/IAI.73.11.7768-7771.2005
    • S. Loisel-Meyer, M.P. Jimenez de Bagues, S. Kohler, J.P. Liautard, and V. Jubier-Maurin Differential use of the two high-oxygen-affinity terminal oxidases of Brucella suis for in vitro and intramacrophagic multiplication Infect. Immun. 73 2005 7768 7771 (Pubitemid 41587684)
    • (2005) Infection and Immunity , vol.73 , Issue.11 , pp. 7768-7771
    • Loisel-Meyer, S.1    Jimenez De Bagues, M.P.2    Kohler, S.3    Liautard, J.-P.4    Jubier-Maurin, V.5
  • 90
    • 0025030204 scopus 로고
    • Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: Mutants deficient in the cytochrome d complex are unable to fix nitrogen in air
    • M.J.S. Kelly, R.K. Poole, M.G. Yates, and C. Kennedy Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air J. Bacteriol. 172 1990 6010 6019 (Pubitemid 20317143)
    • (1990) Journal of Bacteriology , vol.172 , Issue.10 , pp. 6010-6019
    • Kelly, M.J.S.1    Poole, R.K.2    Yates, M.G.3    Kennedy, C.4
  • 92
    • 0025057311 scopus 로고
    • The purification, characterization and role of the d-type cytochrome oxidase of Klebsiella pneumoniae during nitrogen fixation
    • A. Smith, S. Hill, and C. Anthony The purification, characterization and role of the d-type cytochrome oxidase of Klebsiella pneumoniae during nitrogen fixation J. Gen. Microbiol. 136 1990 171 180 (Pubitemid 20045984)
    • (1990) Journal of General Microbiology , vol.136 , Issue.1 , pp. 171-180
    • Smith, A.1    Hill, S.2    Anthony, C.3
  • 93
    • 0028263624 scopus 로고
    • Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghaemoglobin and oxymyoglobin: Cytochrome bd is a low-affinity oxidase
    • R. D'Mello, S. Hill, and R.K. Poole Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghaemoglobin and oxymyoglobin: cytochrome bd is a low-affinity oxidase Microbiology 140 1994 1395 1402 (Pubitemid 24195911)
    • (1994) Microbiology , vol.140 , Issue.6 , pp. 1395-1402
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 95
    • 0030812874 scopus 로고    scopus 로고
    • The Klebsiella pneumoniae cytochrome bd' terminal oxidase complex and its role in microaerobic nitrogen fixation
    • N.S. Juty, F. Moshiri, M. Merrick, C. Anthony, and S. Hill The Klebsiella pneumoniae cytochrome bd' terminal oxidase complex and its role in microaerobic nitrogen fixation Microbiology 143 1997 2673 2683 (Pubitemid 27389953)
    • (1997) Microbiology , vol.143 , Issue.8 , pp. 2673-2683
    • Juty, N.S.1    Moshiri, F.2    Merrick, M.3    Anthony, C.4    Hill, S.5
  • 96
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii - Roles of the terminal oxidases
    • R.K. Poole, and S. Hill Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases Biosci. Rep. 17 1997 307 317
    • (1997) Biosci. Rep. , vol.17 , pp. 307-317
    • Poole, R.K.1    Hill, S.2
  • 97
    • 65949120626 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase complex in Azotobacter vinelandii
    • Y.V. Bertsova, O.V. Demin, and A.V. Bogachev Respiratory protection of nitrogenase complex in Azotobacter vinelandii Usp. Biol. Khim. (in Russian) 45 2005 205 234
    • (2005) Usp. Biol. Khim. (In Russian) , vol.45 , pp. 205-234
    • Bertsova, Y.V.1    Demin, O.V.2    Bogachev, A.V.3
  • 98
    • 79952446885 scopus 로고    scopus 로고
    • Bd oxidase homologue of photosynthetic purple sulfur bacterium Allochromatium vinosum is co-transcribed with a nitrogen fixation related gene
    • H.B. Dincturk, V. Demir, and T. Aykanat Bd oxidase homologue of photosynthetic purple sulfur bacterium Allochromatium vinosum is co-transcribed with a nitrogen fixation related gene Antonie Van Leeuwenhoek 99 2011 211 220
    • (2011) Antonie Van Leeuwenhoek , vol.99 , pp. 211-220
    • Dincturk, H.B.1    Demir, V.2    Aykanat, T.3
  • 99
    • 77953734607 scopus 로고    scopus 로고
    • Adaptation to oxygen: Role of terminal oxidases in photosynthesis initiation in the purple photosynthetic bacterium, Rubrivivax gelatinosus
    • B.K. Hassani, A.S. Steunou, S. Liotenberg, F. Reiss-Husson, C. Astier, and S. Ouchane Adaptation to oxygen: role of terminal oxidases in photosynthesis initiation in the purple photosynthetic bacterium, Rubrivivax gelatinosus J. Biol. Chem. 285 2010 19891 19899
    • (2010) J. Biol. Chem. , vol.285 , pp. 19891-19899
    • Hassani, B.K.1    Steunou, A.S.2    Liotenberg, S.3    Reiss-Husson, F.4    Astier, C.5    Ouchane, S.6
  • 100
    • 0032989878 scopus 로고    scopus 로고
    • Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence
    • S.S. Way, S. Sallustio, R.S. Magliozzo, and M.B. Goldberg Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence J. Bacteriol. 181 1999 1229 1237 (Pubitemid 29119562)
    • (1999) Journal of Bacteriology , vol.181 , Issue.4 , pp. 1229-1237
    • Way, S.S.1    Sallustio, S.2    Magliozzo, R.S.3    Goldberg, M.B.4
  • 101
    • 0035089129 scopus 로고    scopus 로고
    • Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection
    • DOI 10.1128/JB.183.8.2454-2462.2001
    • S. Endley, D. McMurray, and T.A. Ficht Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection J. Bacteriol. 183 2001 2454 2462 (Pubitemid 32249753)
    • (2001) Journal of Bacteriology , vol.183 , Issue.8 , pp. 2454-2462
    • Endley, S.1    McMurray, D.2    Ficht, T.A.3
  • 102
    • 17144388984 scopus 로고    scopus 로고
    • Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence
    • DOI 10.1111/j.1365-2958.2005.04555.x
    • Y. Yamamoto, C. Poyart, P. Trieu-Cuot, G. Lamberet, A. Gruss, and P. Gaudu Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence Mol. Microbiol. 56 2005 525 534 (Pubitemid 40516788)
    • (2005) Molecular Microbiology , vol.56 , Issue.2 , pp. 525-534
    • Yamamoto, Y.1    Poyart, C.2    Trieu-Cuot, P.3    Lamberet, G.4    Gruss, A.5    Gaudu, P.6
  • 103
    • 0030778203 scopus 로고    scopus 로고
    • Influence of genes encoding proton-translocating enzymes on suppression of Salmonella typhimurium growth and colonization
    • L. Zhang-Barber, A.K. Turner, G. Martin, G. Frankel, G. Dougan, and P.A. Barrow Influence of genes encoding proton-translocating enzymes on suppression of Salmonella typhimurium growth and colonization J. Bacteriol. 179 1997 7186 7190 (Pubitemid 27492508)
    • (1997) Journal of Bacteriology , vol.179 , Issue.22 , pp. 7186-7190
    • Zhang-Barber, L.1    Turner, A.K.2    Martin, G.3    Frankel, G.4    Dougan, G.5    Barrow, P.A.6
  • 104
    • 0038781764 scopus 로고    scopus 로고
    • Contribution of proton-translocating proteins to the virulence of Salmonella enterica serovars Typhimurium, Gallinarum, and Dublin in chickens and mice
    • DOI 10.1128/IAI.71.6.3392-3401.2003
    • A.K. Turner, L.Z. Barber, P. Wigley, S. Muhammad, M.A. Jones, M.A. Lovell, S. Hulme, and P.A. Barrow Contribution of proton-translocating proteins to the virulence of Salmonella enterica Serovars Typhimurium, Gallinarum, and Dublin in chickens and mice Infect. Immun. 71 2003 3392 3401 (Pubitemid 36637567)
    • (2003) Infection and Immunity , vol.71 , Issue.6 , pp. 3392-3401
    • Turner, A.K.1    Barber, L.Z.2    Wigley, P.3    Muhammad, S.4    Jones, M.A.5    Lovell, M.A.6    Hulme, S.7    Barrow, P.A.8
  • 105
    • 33748517887 scopus 로고    scopus 로고
    • The response regulator ResD modulates virulence gene expression in response to carbohydrates in Listeria monocytogenes
    • DOI 10.1111/j.1365-2958.2006.05328.x
    • M.H. Larsen, B.H. Kallipolitis, J.K. Christiansen, J.E. Olsen, and H. Ingmer The response regulator ResD modulates virulence gene expression in response to carbohydrates in Listeria monocytogenes Mol. Microbiol. 61 2006 1622 1635 (Pubitemid 44359388)
    • (2006) Molecular Microbiology , vol.61 , Issue.6 , pp. 1622-1635
    • Larsen, M.H.1    Kallipolitis, B.H.2    Christiansen, J.K.3    Olsen, J.E.4    Ingmer, H.5
  • 106
    • 4944233196 scopus 로고    scopus 로고
    • Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide
    • DOI 10.1016/j.febslet.2004.09.013, PII S0014579304011275
    • V.B. Borisov, E. Forte, A.A. Konstantinov, R.K. Poole, P. Sarti, and A. Giuffrè Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide FEBS Lett. 576 2004 201 204 (Pubitemid 39330483)
    • (2004) FEBS Letters , vol.576 , Issue.1-2 , pp. 201-204
    • Borisov, V.B.1    Forte, E.2    Konstantinov, A.A.3    Poole, R.K.4    Sarti, P.5    Giuffre, A.6
  • 111
    • 67651098870 scopus 로고    scopus 로고
    • Reaction of nitric oxide with the oxidized di-heme and heme-copper oxygen-reducing centers of terminal oxidases: Different reaction pathways and end-products
    • V.B. Borisov, E. Forte, A. Giuffrè, A. Konstantinov, and P. Sarti Reaction of nitric oxide with the oxidized di-heme and heme-copper oxygen-reducing centers of terminal oxidases: different reaction pathways and end-products J. Inorg. Biochem. 103 2009 1185 1187
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 1185-1187
    • Borisov, V.B.1    Forte, E.2    Giuffrè, A.3    Konstantinov, A.4    Sarti, P.5
  • 112
  • 113
    • 77951684325 scopus 로고    scopus 로고
    • Peroxidase activity of cytochrome bd from Escherichia coli
    • (translated from Biokhimiya (in Russian) (2010), 75, 520-530)
    • V.B. Borisov, A.I. Davletshin, and A.A. Konstantinov Peroxidase activity of cytochrome bd from Escherichia coli Biochemistry (Moscow) 75 2010 428 436 (translated from Biokhimiya (in Russian) (2010), 75, 520-530)
    • (2010) Biochemistry (Moscow) , vol.75 , pp. 428-436
    • Borisov, V.B.1    Davletshin, A.I.2    Konstantinov, A.A.3
  • 114
    • 77949342990 scopus 로고    scopus 로고
    • Two sources of endogenous hydrogen peroxide in Escherichia coli
    • S. Korshunov, and J.A. Imlay Two sources of endogenous hydrogen peroxide in Escherichia coli Mol. Microbiol. 75 2010 1389 1401
    • (2010) Mol. Microbiol. , vol.75 , pp. 1389-1401
    • Korshunov, S.1    Imlay, J.A.2
  • 115
    • 0035159222 scopus 로고    scopus 로고
    • Extracellular superoxide production by Enterococcus faecalis requires demethylmenaquinone and is attenuated by functional terminal quinol oxidases
    • DOI 10.1046/j.1365-2958.2001.02638.x
    • M.M. Huycke, D. Moore, W. Joyce, P. Wise, L. Shepard, Y. Kotake, and M.S. Gilmore Extracellular superoxide production by Enterococcus faecalis requires demethylmenaquinone and is attenuated by functional terminal quinol oxidases Mol. Microbiol. 42 2001 729 740 (Pubitemid 33064482)
    • (2001) Molecular Microbiology , vol.42 , Issue.3 , pp. 729-740
    • Huycke, M.M.1    Moore, D.2    Joyce, W.3    Wise, P.4    Shepard, L.5    Kotake, Y.6    Gilmore, M.S.7
  • 117
    • 0034177441 scopus 로고    scopus 로고
    • Mutation of cytochrome bd quinol oxidase results in reduced stationary phase survival, iron deprivation, metal toxicity and oxidative stress in Azotobacter vinelandii
    • DOI 10.1016/S0378-1097(00)00073-2, PII S0378109700000732
    • S.E. Edwards, C.S. Loder, G. Wu, H. Corker, B.W. Bainbridge, S. Hill, and R.K. Poole Mutation of cytochrome bd quinol oxidase results in reduced stationary phase survival, iron deprivation, metal toxicity and oxidative stress in Azotobacter vinelandii FEMS Microbiol. Lett. 185 2000 71 77 (Pubitemid 30145609)
    • (2000) FEMS Microbiology Letters , vol.185 , Issue.1 , pp. 71-77
    • Edwards, S.E.1    Loder, C.S.2    Wu, G.3    Corker, H.4    Bainbridge, B.W.5    Hill, S.6    Poole, R.K.7
  • 118
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • DOI 10.1016/S0092-8674(00)81016-8
    • M. Bader, W. Muse, D.P. Ballou, C. Gassner, and J.C.A. Bardwell Oxidative protein folding is driven by the electron transport system Cell 98 1999 217 227 (Pubitemid 29344909)
    • (1999) Cell , vol.98 , Issue.2 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.A.5
  • 120
    • 0017858515 scopus 로고
    • Oxygen limited continuous culture and respiratory energy conservation in Escherichia coli
    • C.W. Rice, and W.P. Hempfling Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli J. Bacteriol. 134 1978 115 124 (Pubitemid 8334694)
    • (1978) Journal of Bacteriology , vol.134 , Issue.1 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 121
    • 0025129999 scopus 로고
    • Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH and the fnr gene product
    • P.A. Cotter, V. Chepuri, R.B. Gennis, and R.P. Gunsalus Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product J. Bacteriol. 172 1990 6333 6338 (Pubitemid 20372773)
    • (1990) Journal of Bacteriology , vol.172 , Issue.11 , pp. 6333-6338
    • Cotter, P.A.1    Chepuri, V.2    Gennis, R.B.3    Gunsalus, R.P.4
  • 122
    • 0025754390 scopus 로고
    • The requirement of ArcA and Fnr for peak expression of the cyd operon in Escherichia coli under microaerobic conditions
    • H.-A. Fu, S. Iuchi, and E.C.C. Lin The requirement of ArcA and Fnr for peak expression of the cyd operon in Escherichia coli under microaerobic conditions Mol. Gen. Genet. 226 1991 209 213
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 209-213
    • Fu, H.-A.1    Iuchi, S.2    Lin, E.C.C.3
  • 124
    • 0026646181 scopus 로고
    • Arc-Dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon
    • D. Wall, J.M. Delaney, O. Fayet, B. Lipinska, T. Yamamoto, and C. Georgopoulos arc-Dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon J. Bacteriol. 174 1992 6554 6562
    • (1992) J. Bacteriol. , vol.174 , pp. 6554-6562
    • Wall, D.1    Delaney, J.M.2    Fayet, O.3    Lipinska, B.4    Yamamoto, T.5    Georgopoulos, C.6
  • 125
    • 0027391503 scopus 로고
    • Molecular characterization of the Escherichia coli htrD gene: Cloning, sequence, regulation, and involvement with cytochrome d oxidase
    • J.M. Delaney, D. Wall, and C. Georgopoulos Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase J. Bacteriol. 175 1993 166 175 (Pubitemid 23016663)
    • (1993) Journal of Bacteriology , vol.175 , Issue.1 , pp. 166-175
    • Delaney, J.M.1    Wall, D.2    Georgopoulos, C.3
  • 126
    • 0016700183 scopus 로고
    • Synthesis of alternative membrane-bound redox carriers during aerobic growth of Escherichia coli in the presence of potassium cyanide
    • J.R. Ashcroft, and B.A. Haddock Synthesis of alternative membrane-bound redox carriers during aerobic growth of Escherichia coli in the presence of potassium cyanide Biochem. J. 148 1975 349 352
    • (1975) Biochem. J. , vol.148 , pp. 349-352
    • Ashcroft, J.R.1    Haddock, B.A.2
  • 127
    • 0141737064 scopus 로고    scopus 로고
    • + redox poise in Streptomyces coelicolor A3(2)
    • DOI 10.1093/emboj/cdg453
    • + redox poise in Streptomyces coelicolor A3(2) EMBO J. 22 2003 4856 4865 (Pubitemid 37162921)
    • (2003) EMBO Journal , vol.22 , Issue.18 , pp. 4856-4865
    • Brekasis, D.1    Paget, M.S.B.2
  • 128
    • 0027439091 scopus 로고
    • Cytochrome d induction in Escherichia coli growing under unfavorable conditions
    • DOI 10.1016/0014-5793(93)81612-4
    • A.V. Bogachev, R.A. Murtazina, and V.P. Skulachev Cytochrome d induction in Escherichia coli growing under unfavorable conditions FEBS Lett. 336 1993 75 78 (Pubitemid 23362006)
    • (1993) FEBS Letters , vol.336 , Issue.1 , pp. 75-78
    • Bogachev, A.V.1    Murtazina, R.A.2    Skulachev, V.P.3
  • 131
    • 21744460518 scopus 로고    scopus 로고
    • Pressure-regulated biosynthesis of cytochrome bd in piezo- and psychrophilic deep-sea bacterium Shewanella violacea DSS12
    • DOI 10.1007/s00792-005-0439-2
    • H. Tamegai, H. Kawano, A. Ishii, S. Chikuma, K. Nakasone, and C. Kato Pressure-regulated biosynthesis of cytochrome bd in piezo- and psychrophilic deep-sea bacterium Shewanella violacea DSS12 Extremophiles 9 2005 247 253 (Pubitemid 40938367)
    • (2005) Extremophiles , vol.9 , Issue.3 , pp. 247-253
    • Tamegai, H.1    Kawano, H.2    Ishii, A.3    Chikuma, S.4    Nakasone, K.5    Kato, C.6
  • 132
    • 17944386101 scopus 로고
    • Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: Identification and mapping of a fourth locus, cydD
    • R.K. Poole, H.D. Williams, J.A. Downie, and F. Gibson Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: identification and mapping of a fourth locus, cydD J. Gen. Microbiol. 135 1989 1865 1874
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1865-1874
    • Poole, R.K.1    Williams, H.D.2    Downie, J.A.3    Gibson, F.4
  • 133
    • 0030034751 scopus 로고    scopus 로고
    • AarD, a Providencia stuartii homologue of cydD: Role in 2′-N-acetyltransferase expression, cell morphology and growth in the presence of an extracellular factor
    • D.R. Macinga, and P.N. Rather aarD, a Providencia stuartii homologue of cydD: role in 2′-N-acetyltransferase expression, cell morphology and growth in the presence of an extracellular factor Mol. Microbiol. 19 1996 511 520
    • (1996) Mol. Microbiol. , vol.19 , pp. 511-520
    • MacInga, D.R.1    Rather, P.N.2
  • 134
    • 0032407979 scopus 로고    scopus 로고
    • A factor produced by Escherichia coli K-12 inhibits the growth of E. Coli mutants defective in the cytochrome bd quinol oxidase complex: Enterochelin rediscovered
    • G.M. Cook, C. Loder, B. Soballe, G.P. Stafford, J. Membrillo-Hernandez, and R.K. Poole A factor produced by Escherichia coli K-12 inhibits the growth of
    • (1998) Microbiology , vol.144 , Issue.12 , pp. 3297-3308
    • Cook, G.M.1    Loder, C.2    Soballe, B.3    Stafford, G.P.4    Membrillo-Hernandez, J.5    Poole, R.K.6
  • 135
    • 0027715744 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant defective in resuming growth after starvation
    • D.A. Siegele, and R. Kolter Isolation and characterization of an Escherichia coli mutant defective in resuming growth after starvation Genes Dev. 7 1993 2629 2640 (Pubitemid 24021019)
    • (1993) Genes and Development , vol.7 , Issue.12 , pp. 2629-2640
    • Siegele, D.A.1    Kolter, R.2
  • 136
    • 0029858145 scopus 로고    scopus 로고
    • The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase
    • D.A. Siegele, K.R. Imlay, and J.A. Imlay The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase J. Bacteriol. 178 1996 6091 6096 (Pubitemid 26365684)
    • (1996) Journal of Bacteriology , vol.178 , Issue.21 , pp. 6091-6096
    • Siegele, D.A.1    Imlay, K.R.C.2    Imlay, J.A.3
  • 137
    • 58649098300 scopus 로고    scopus 로고
    • Antibiotics LL-Z1272 identified as novel inhibitors discriminating bacterial and mitochondrial quinol oxidases
    • T. Mogi, H. Ui, K. Shiomi, S. Omura, H. Miyoshi, and K. Kita Antibiotics LL-Z1272 identified as novel inhibitors discriminating bacterial and mitochondrial quinol oxidases Biochim. Biophys. Acta 1787 2009 129 133
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 129-133
    • Mogi, T.1    Ui, H.2    Shiomi, K.3    Omura, S.4    Miyoshi, H.5    Kita, K.6
  • 138
    • 70849102756 scopus 로고    scopus 로고
    • Gramicidin S and polymyxins: The revival of cationic cyclic peptide antibiotics
    • T. Mogi, and K. Kita Gramicidin S and polymyxins: the revival of cationic cyclic peptide antibiotics Cell. Mol. Life Sci. 66 2009 3821 3826
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3821-3826
    • Mogi, T.1    Kita, K.2
  • 139
    • 0036803070 scopus 로고    scopus 로고
    • Defects in mitochondrial respiratory complexes III and IV, and human pathologies
    • DOI 10.1016/S0098-2997(02)00013-4, PII S0098299702000134
    • V.B. Borisov Defects in mitochondrial respiratory complexes III and IV, and human pathologies Mol. Aspects Med. 23 2002 385 412 (Pubitemid 35286653)
    • (2002) Molecular Aspects of Medicine , vol.23 , Issue.5 , pp. 385-412
    • Borisov, V.B.1
  • 140
    • 16644362431 scopus 로고    scopus 로고
    • Mutations in respiratory chain complexes and human diseases
    • V.B. Borisov Mutations in respiratory chain complexes and human diseases Ital. J. Biochem. 53 2004 34 40
    • (2004) Ital. J. Biochem. , vol.53 , pp. 34-40
    • Borisov, V.B.1
  • 141
    • 64049108876 scopus 로고    scopus 로고
    • Assembly of a chimeric respiratory chain from bovine heart submitochondrial particles and cytochrome bd terminal oxidase of Escherichia coli
    • E.V. Gavrikova, V.G. Grivennikova, V.B. Borisov, G. Cecchini, and A.D. Vinogradov Assembly of a chimeric respiratory chain from bovine heart submitochondrial particles and cytochrome bd terminal oxidase of Escherichia coli FEBS Lett. 583 2009 1287 1291
    • (2009) FEBS Lett. , vol.583 , pp. 1287-1291
    • Gavrikova, E.V.1    Grivennikova, V.G.2    Borisov, V.B.3    Cecchini, G.4    Vinogradov, A.D.5
  • 144
    • 70450277400 scopus 로고    scopus 로고
    • The alternative oxidase, a tool for compensating cytochrome c oxidase deficiency in human cells
    • E.P. Dassa, E. Dufour, S. Goncalves, H.T. Jacobs, and P. Rustin The alternative oxidase, a tool for compensating cytochrome c oxidase deficiency in human cells Physiol. Plant. 137 2009 427 434
    • (2009) Physiol. Plant. , vol.137 , pp. 427-434
    • Dassa, E.P.1    Dufour, E.2    Goncalves, S.3    Jacobs, H.T.4    Rustin, P.5
  • 145
    • 44749089929 scopus 로고    scopus 로고
    • Gramicidin S identified as a potent inhibitor for cytochrome bd-type quinol oxidase
    • T. Mogi, H. Ui, K. Shiomi, S. Omura, and K. Kita Gramicidin S identified as a potent inhibitor for cytochrome bd-type quinol oxidase FEBS Lett. 582 2008 2299 2302
    • (2008) FEBS Lett. , vol.582 , pp. 2299-2302
    • Mogi, T.1    Ui, H.2    Shiomi, K.3    Omura, S.4    Kita, K.5
  • 146
    • 0026129552 scopus 로고
    • E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli
    • M.W. Calhoun, G. Newton, and R.B. Gennis E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli J. Bacteriol. 173 1991 1569 1570
    • (1991) J. Bacteriol. , vol.173 , pp. 1569-1570
    • Calhoun, M.W.1    Newton, G.2    Gennis, R.B.3
  • 147
    • 0021039982 scopus 로고
    • Immunological characterization of an Escherichia coli strain which is lacking cytochrome d
    • R.G. Kranz, C.A. Barassi, M.J. Miller, G.N. Green, and R.B. Gennis Immunological characterization of an E. coli strain which is lacking cytochrome d J. Bacteriol. 156 1983 115 121 (Pubitemid 14227357)
    • (1983) Journal of Bacteriology , vol.156 , Issue.1 , pp. 115-121
    • Kranz, R.G.1    Barassi, C.A.2    Miller, M.J.3
  • 148
    • 0025365339 scopus 로고
    • Linkage map of Escherichia coli K-12, Edition 8
    • B.J. Bachmann Linkage map of Escherichia coli K-12, Edition 8 Microbiol. Rev. 54 1990 130 197
    • (1990) Microbiol. Rev. , vol.54 , pp. 130-197
    • Bachmann, B.J.1
  • 149
    • 0021690885 scopus 로고
    • Cloning the cyd gene locus coding for the cytochrome d complex of Escherichia coli
    • DOI 10.1016/0378-1119(84)90037-4
    • G.N. Green, J.E. Kranz, and R.B. Gennis Cloning the cyd gene locus coding for the cytochrome d complex of Escherichia coli Gene 32 1984 99 106 (Pubitemid 15196402)
    • (1984) Gene , vol.32 , Issue.1-2 , pp. 99-106
    • Green, G.N.1    Kranz, J.E.2    Gennis, R.B.3
  • 151
    • 0025805327 scopus 로고
    • In vivo assembly of the cytochrome d terminal oxidase complex of Escherichia coli from genes encoding the two subunits expressed on separate plasmids
    • G. Newton, and R.B. Gennis In vivo assembly of the cytochrome d terminal oxidase complex of Escherichia coli from genes encoding the two subunits expressed on separate plasmids Biochim. Biophys. Acta 1089 1991 8 12
    • (1991) Biochim. Biophys. Acta , vol.1089 , pp. 8-12
    • Newton, G.1    Gennis, R.B.2
  • 152
    • 0022542231 scopus 로고
    • 558 component of the cytochrome d complex from Escherichia coli
    • 558 component of the cytochrome d complex from Escherichia coli Biochemistry 25 1986 2309 2314 (Pubitemid 16075199)
    • (1986) Biochemistry , vol.25 , Issue.9 , pp. 2309-2314
    • Green, G.N.1    Lorence, R.M.2    Gennis, R.B.3
  • 153
    • 0023276114 scopus 로고
    • Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli
    • C.D. Georgiou, H. Fang, and R.B. Gennis Identification of the cydC locus required for the expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli J. Bacteriol. 169 1987 2107 2112 (Pubitemid 17081775)
    • (1987) Journal of Bacteriology , vol.169 , Issue.5 , pp. 2107-2112
    • Georgiou, C.D.1    Fang, H.2    Gennis, R.B.3
  • 154
    • 0027489253 scopus 로고
    • Cytochrome bd biosynthesis in Escherichia coli: The sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter
    • R.K. Poole, L. Hatch, M.W.J. Cleeter, F. Gibson, G.B. Cox, and G. Wu Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter Mol. Microbiol. 10 1993 421 430 (Pubitemid 23316751)
    • (1993) Molecular Microbiology , vol.10 , Issue.2 , pp. 421-430
    • Poole, R.K.1    Hatch, L.2    Cleeter, M.W.J.3    Gibson, F.4    Cox, G.B.5    Wu, G.6
  • 155
    • 0027303826 scopus 로고
    • Investigation of the role of the cydD gene product in production of a functional cytochrome d oxidase in Escherichia coli
    • DOI 10.1016/0378-1097(93)90531-6
    • K.J. Bebbington, and H.D. Williams Investigation of the role of the cydD gene product in production of a functional cytochrome d oxidase in Escherichia coli FEMS Microbiol. Lett. 112 1993 19 24 (Pubitemid 23257997)
    • (1993) FEMS Microbiology Letters , vol.112 , Issue.1 , pp. 19-24
    • Bebbington, K.J.1    Williams, H.D.2
  • 156
    • 0028177039 scopus 로고
    • The cydD gene product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli
    • DOI 10.1016/0378-1097(94)90198-8
    • R.K. Poole, F. Gibson, and G. Wu The cydD gene product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli FEMS Microbiol. Lett. 117 1994 217 224 (Pubitemid 2062778)
    • (1994) FEMS Microbiology Letters , vol.117 , Issue.2 , pp. 217-224
    • Poole, R.K.1    Gibson, F.2    Wu Guanghui3
  • 157
    • 25444517605 scopus 로고    scopus 로고
    • A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm
    • DOI 10.1074/jbc.M503075200
    • M.S. Pittman, H.C. Robinson, and R.K. Poole A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm J. Biol. Chem. 280 2005 32254 32261 (Pubitemid 41361833)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32254-32261
    • Pittman, M.S.1    Robinson, H.C.2    Poole, R.K.3
  • 159
    • 33746538247 scopus 로고    scopus 로고
    • Role of a putative third subunit YhcB on the assembly and function of cytochrome bd-type ubiquinol oxidase from Escherichia coli
    • DOI 10.1016/j.bbabio.2006.05.043, PII S0005272806001757
    • T. Mogi, E. Mizuochi-Asai, S. Endou, S. Akimoto, and H. Nakamura Role of a putative third subunit YhcB on the assembly and function of cytochrome bd-type ubiquinol oxidase from Escherichia coli Biochim. Biophys. Acta 1757 2006 860 864 (Pubitemid 44142426)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.7 , pp. 860-864
    • Mogi, T.1    Mizuochi-Asai, E.2    Endou, S.3    Akimoto, S.4    Nakamura, H.5
  • 160
    • 0026006133 scopus 로고
    • A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA)
    • J. Dassa, H. Fsihi, C. Marck, M. Dion, M. Kieffer-Bontemps, and P.L. Boquet A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA) Mol. Gen. Genet. 229 1991 341 352
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 341-352
    • Dassa, J.1    Fsihi, H.2    Marck, C.3    Dion, M.4    Kieffer-Bontemps, M.5    Boquet, P.L.6
  • 161
    • 0030067649 scopus 로고    scopus 로고
    • Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli
    • C.-P. Tseng, J. Albrecht, and R.P. Gunsalus Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli J. Bacteriol. 178 1996 1094 1098 (Pubitemid 26048026)
    • (1996) Journal of Bacteriology , vol.178 , Issue.4 , pp. 1094-1098
    • Tseng, C.-P.1    Albrecht, J.2    Gunsalus, R.P.3
  • 162
    • 0036177861 scopus 로고    scopus 로고
    • Quantitative assessment of oxygen availability: Perceived aerobiosis and its effect on flux distribution in the respiratory chain of Escherichia coli
    • S. Alexeeva, K. Hellingwerf, and M.J. Teixeira de Mattos Quantitative assessment of oxygen availability: perceived aerobiosis and its effect on flux distribution in the respiratory chain of Escherichia coli J. Bacteriol. 184 2002 1402 1406 (Pubitemid 34157563)
    • (2002) Journal of Bacteriology , vol.184 , Issue.5 , pp. 1402-1406
    • Alexeeva, S.1    Hellingwerf, K.J.2    Teixeira De Mattos, M.J.3
  • 163
    • 0025144171 scopus 로고
    • Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: Study utilizing deletions and lac fusions of cyo and cyd
    • S. Iuchi, V. Chepuri, H.A. Fu, R.B. Gennis, and E.C. Lin Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: study utilizing deletions and lac fusions of cyo and cyd J. Bacteriol. 172 1990 6020 6025 (Pubitemid 20317144)
    • (1990) Journal of Bacteriology , vol.172 , Issue.10 , pp. 6020-6025
    • Iuchi, S.1    Chepuri, V.2    Fu, H.-A.3    Gennis, R.B.4    Lin, E.C.C.5
  • 164
    • 0026813814 scopus 로고
    • Contribution of the fnr and arcA gene products in coordinate regulation of cytochrome o and d oxidase (cyoABCDE and cydAB) genes in Escherichia coli
    • P.A. Cotter, and R.P. Gunsalus Contribution of the fnr and arcA gene products in coordinate regulation of cytochrome o and d oxidase (cyoABCDE and cydAB) genes in Escherichia coli FEMS Microbiol. Lett. 91 1992 31 36
    • (1992) FEMS Microbiol. Lett. , vol.91 , pp. 31-36
    • Cotter, P.A.1    Gunsalus, R.P.2
  • 165
    • 0026539733 scopus 로고
    • Control of electron flow in Escherichia coli: Coordinated transcription of respiratory pathway genes
    • R.P. Gunsalus Control of electron flow in Escherichia coli: coordinated transcription of respiratory pathway genes J. Bacteriol. 174 1992 7069 7074
    • (1992) J. Bacteriol. , vol.174 , pp. 7069-7074
    • Gunsalus, R.P.1
  • 166
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • DOI 10.1016/S0005-2728(97)00034-0, PII S0005272897000340
    • G. Unden, and J. Bongaerts Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors Biochim. Biophys. Acta 1320 1997 217 234 (Pubitemid 27283364)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1320 , Issue.3 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 167
    • 0030764901 scopus 로고    scopus 로고
    • Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: Roles of Fnr and Arca in repression and activation
    • P.A. Cotter, S.B. Melville, J.A. Albrecht, and R.P. Gunsalus Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: roles of Fnr and ArcA in repression and activation Mol. Microbiol. 25 1997 605 615 (Pubitemid 27373588)
    • (1997) Molecular Microbiology , vol.25 , Issue.3 , pp. 605-615
    • Cotter, P.A.1    Melville, S.B.2    Albrecht, J.A.3    Gunsalus, R.P.4
  • 168
    • 0033781828 scopus 로고    scopus 로고
    • Oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operon: Roles of multiple promoters and the Fnr-1 and Fnr-2 binding sites
    • F. Govantes, J.A. Albrecht, and R.P. Gunsalus Oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operon: roles of multiple promoters and the Fnr-1 and Fnr-2 binding sites Mol. Microbiol. 37 2000 1456 1469
    • (2000) Mol. Microbiol. , vol.37 , pp. 1456-1469
    • Govantes, F.1    Albrecht, J.A.2    Gunsalus, R.P.3
  • 169
    • 29044445103 scopus 로고    scopus 로고
    • Effect of oxygen, and ArcA and FNR regulators on the expression of genes related to the electron transfer chain and the TCA cycle in Escherichia coli
    • DOI 10.1016/j.ymben.2005.07.001, PII S1096717605000558
    • S. Shalel-Levanon, K.Y. San, and G.N. Bennett Effect of oxygen, and ArcA and FNR regulators on the expression of genes related to the electron transfer chain and the TCA cycle in Escherichia coli Metab. Eng. 7 2005 364 374 (Pubitemid 41790467)
    • (2005) Metabolic Engineering , vol.7 , Issue.5-6 , pp. 364-374
    • Shalel-Levanon, S.1    San, K.-Y.2    Bennett, G.N.3
  • 171
    • 0035933597 scopus 로고    scopus 로고
    • Quinones as the redox signal for the Arc two-component system of bacteria
    • DOI 10.1126/science.1059361
    • D. Georgellis, O. Kwon, and E.C. Lin Quinones as the redox signal for the arc two-component system of bacteria Science 292 2001 2314 2316 (Pubitemid 32568050)
    • (2001) Science , vol.292 , Issue.5525 , pp. 2314-2316
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.C.3
  • 172
    • 0033544879 scopus 로고    scopus 로고
    • Amplification of signaling activity of the Arc two-component system of Escherichia coli by anaerobic metabolites: An in vitro study with different protein modules
    • D. Georgellis, O. Kwon, and E.C. Lin Amplification of signaling activity of the arc two-component system of Escherichia coli by anaerobic metabolites. An in vitro study with different protein modules J. Biol. Chem. 274 1999 35950 35954 (Pubitemid 129512904)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.50 , pp. 35950-35954
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.C.3
  • 173
    • 0037216801 scopus 로고    scopus 로고
    • Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions
    • DOI 10.1128/JB.185.1.204-209.2003
    • S. Alexeeva, K.J. Hellingwerf, and M.J. Teixeira de Mattos Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions J. Bacteriol. 185 2003 204 209 (Pubitemid 36008838)
    • (2003) Journal of Bacteriology , vol.185 , Issue.1 , pp. 204-209
    • Alexeeva, S.1    Hellingwerf, K.J.2    Teixeira De Mattos, M.J.3
  • 174
    • 0032457906 scopus 로고    scopus 로고
    • Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster
    • DOI 10.1016/S0168-6445(98)00022-9, PII S0168644598000229
    • P.J. Kiley, and H. Beinert Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster FEMS Microbiol. Rev. 22 1998 341 352 (Pubitemid 29074341)
    • (1998) FEMS Microbiology Reviews , vol.22 , Issue.5 , pp. 341-352
    • Kiley, P.J.1    Beinert, H.2
  • 175
    • 32544461820 scopus 로고    scopus 로고
    • Microarray analysis of gene regulation by oxygen, nitrate, nitrite, FNR, NarL and NarP during anaerobic growth of Escherichia coli: New insights into microbial physiology
    • DOI 10.1042/BST0340104
    • T.W. Overton, L. Griffiths, M.D. Patel, J.L. Hobman, C.W. Penn, J.A. Cole, and C. Constantinidou Microarray analysis of gene regulation by oxygen, nitrate, nitrite, FNR, NarL and NarP during anaerobic growth of Escherichia coli: new insights into microbial physiology Biochem. Soc. Trans. 34 2006 104 107 (Pubitemid 43235545)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.1 , pp. 104-107
    • Overton, T.W.1    Griffiths, L.2    Patel, M.D.3    Hobman, J.L.4    Penn, C.W.5    Cole, J.A.6    Constantinidou, C.7
  • 177
    • 0028106110 scopus 로고
    • Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase
    • T. Atlung, and L. Brøndsted Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase J. Bacteriol. 176 1994 5414 5422 (Pubitemid 24273531)
    • (1994) Journal of Bacteriology , vol.176 , Issue.17 , pp. 5414-5422
    • Atlung, T.1    Brondsted, L.2
  • 178
    • 0029866860 scopus 로고    scopus 로고
    • Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli
    • L. Brøndsted, and T. Atlung Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli J. Bacteriol. 178 1996 1556 1564
    • (1996) J. Bacteriol. , vol.178 , pp. 1556-1564
    • Brøndsted, L.1    Atlung, T.2
  • 179
    • 0029867565 scopus 로고    scopus 로고
    • Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4
    • M.G. Sturr, T.A. Krulwich, and D.B. Hicks Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4 J. Bacteriol. 176 1996 1742 1749 (Pubitemid 26085624)
    • (1996) Journal of Bacteriology , vol.178 , Issue.6 , pp. 1742-1749
    • Sturr, M.G.1    Krulwich, T.A.2    Hicks, D.B.3
  • 180
    • 68949158532 scopus 로고    scopus 로고
    • Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase
    • M. Bekker, S. de Vries, A. Ter Beek, K.J. Hellingwerf, and M.J. de Mattos Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase J. Bacteriol. 191 2009 5510 5517
    • (2009) J. Bacteriol. , vol.191 , pp. 5510-5517
    • Bekker, M.1    De Vries, S.2    Ter Beek, A.3    Hellingwerf, K.J.4    De Mattos, M.J.5
  • 181
    • 77953298121 scopus 로고    scopus 로고
    • Compensations for diminished terminal oxidase activity in Escherichia coli: Cytochrome bd-II-mediated respiration and glutamate metabolism
    • M. Shepherd, G. Sanguinetti, G.M. Cook, and R.K. Poole Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism J. Biol. Chem. 285 2010 18464 18472
    • (2010) J. Biol. Chem. , vol.285 , pp. 18464-18472
    • Shepherd, M.1    Sanguinetti, G.2    Cook, G.M.3    Poole, R.K.4
  • 182
    • 0034681330 scopus 로고    scopus 로고
    • Regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii by CydR (Fnr). Sensitivity to oxygen, reactive oxygen species, and nitric oxide
    • DOI 10.1074/jbc.275.7.4679
    • G. Wu, H. Cruz-Ramos, S. Hill, J. Green, G. Sawers, and R.K. Poole Regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii by CydR (Fnr). Sensitivity to oxygen, reactive oxygen species, and nitric oxide J. Biol. Chem. 275 2000 4679 4686 (Pubitemid 30108854)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4679-4686
    • Wu, G.1    Cruz-Ramos, H.2    Hill, S.3    Green, J.4    Sawers, G.5    Poole, R.K.6
  • 183
    • 3042857779 scopus 로고    scopus 로고
    • Bacillus subtilis YdiH is a direct negative regulator of the cydABCD operon
    • DOI 10.1128/JB.186.14.4585-4595.2004
    • M. Schau, Y. Chen, and F.M. Hulett Bacillus subtilis YdiH is a direct negative regulator of the cydABCD operon J. Bacteriol. 186 2004 4585 4595 (Pubitemid 38891021)
    • (2004) Journal of Bacteriology , vol.186 , Issue.14 , pp. 4585-4595
    • Schau, M.1    Chen, Y.2    Hulett, F.M.3
  • 184
    • 27144540194 scopus 로고    scopus 로고
    • Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis
    • DOI 10.1099/mic.0.28124-0
    • J.T. Larsson, A. Rogstam, and C. von Wachenfeldt Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis Microbiology 151 2005 3323 3335 (Pubitemid 41488915)
    • (2005) Microbiology , vol.151 , Issue.10 , pp. 3323-3335
    • Larsson, J.T.1    Rogstam, A.2    Von Wachenfeldt, C.3
  • 185
    • 34247647600 scopus 로고    scopus 로고
    • Regulators of the Bacillus subtilis cydABCD operon: Identification of a negative regulator, CcpA, and a positive regulator, ResD
    • DOI 10.1128/JB.00050-07
    • A. Puri-Taneja, M. Schau, Y. Chen, and F.M. Hulett Regulators of the Bacillus subtilis cydABCD operon: identification of a negative regulator, CcpA, and a positive regulator, ResD J. Bacteriol. 189 2007 3348 3358 (Pubitemid 46668799)
    • (2007) Journal of Bacteriology , vol.189 , Issue.9 , pp. 3348-3358
    • Puri-Taneja, A.1    Schau, M.2    Chen, Y.3    Hulett, F.M.4
  • 186
    • 0035946912 scopus 로고    scopus 로고
    • The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus
    • DOI 10.1006/jmbi.2001.4652
    • L.R. Swem, S. Elsen, T.H. Bird, D.L. Swem, H.G. Koch, H. Myllykallio, F. Daldal, and C.E. Bauer The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus J. Mol. Biol. 309 2001 121 138 (Pubitemid 32553512)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.1 , pp. 121-138
    • Swem, L.R.1    Elsen, S.2    Bird, T.H.3    Swem, D.L.4    Koch, H.-G.5    Myllykallio, H.6    Daldal, F.7    Bauer, C.E.8
  • 187
    • 0035805166 scopus 로고    scopus 로고
    • The 'strict' anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain
    • DOI 10.1016/S0014-5793(01)02399-7, PII S0014579301023997
    • R.S. Lemos, C.M. Gomes, M. Santana, J. LeGall, A.V. Xavier, and M. Teixeira The 'strict' anaerobe Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain FEBS Lett. 496 2001 40 43 (Pubitemid 32436418)
    • (2001) FEBS Letters , vol.496 , Issue.1 , pp. 40-43
    • Lemos, R.S.1    Gomes, C.M.2    Santana, M.3    LeGall, J.4    Xavier, A.V.5    Teixeira, M.6
  • 188
    • 0036168642 scopus 로고    scopus 로고
    • The quinol:fumarate oxidoreductase from the sulphate reducing bacterium Desulfovibrio gigas: Spectroscopic and redox studies
    • DOI 10.1023/A:1013814619023
    • R.S. Lemos, C.M. Gomes, J. LeGall, A.V. Xavier, and M. Teixeira The quinol:fumarate oxidoreductase from the sulphate reducing bacterium Desulfovibrio gigas: spectroscopic and redox studies J. Bioenerg. Biomembr. 34 2002 21 30 (Pubitemid 34157702)
    • (2002) Journal of Bioenergetics and Biomembranes , vol.34 , Issue.1 , pp. 21-30
    • Lemos, R.S.1    Gomes, C.M.2    LeGall, J.3    Xavier, A.V.4    Teixeira, M.5
  • 189
    • 33645239654 scopus 로고    scopus 로고
    • Characterization and expression analysis of the cytochrome bd oxidase operon from Desulfovibrio gigas
    • P. Machado, R. Felix, R. Rodrigues, S. Oliveira, and C. Rodrigues-Pousada Characterization and expression analysis of the cytochrome bd oxidase operon from Desulfovibrio gigas Curr. Microbiol. 52 2006 274 281
    • (2006) Curr. Microbiol. , vol.52 , pp. 274-281
    • MacHado, P.1    Felix, R.2    Rodrigues, R.3    Oliveira, S.4    Rodrigues-Pousada, C.5
  • 190
    • 44649189139 scopus 로고    scopus 로고
    • Presence and expression of terminal oxygen reductases in strictly anaerobic sulfate-reducing bacteria isolated from salt-marsh sediments
    • M. Santana Presence and expression of terminal oxygen reductases in strictly anaerobic sulfate-reducing bacteria isolated from salt-marsh sediments Anaerobe 14 2008 145 156
    • (2008) Anaerobe , vol.14 , pp. 145-156
    • Santana, M.1
  • 191
    • 14644397208 scopus 로고    scopus 로고
    • Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica
    • DOI 10.1128/JB.187.6.2020-2029.2005
    • A. Das, R. Silaghi-Dumitrescu, L.G. Ljungdahl, and D.M. Kurtz Jr. Cytochrome bd oxidase, oxidative stress, and dioxygen tolerance of the strictly anaerobic bacterium Moorella thermoacetica J. Bacteriol. 187 2005 2020 2029 (Pubitemid 40316232)
    • (2005) Journal of Bacteriology , vol.187 , Issue.6 , pp. 2020-2029
    • Das, A.1    Silaghi-Dumitrescu, R.2    Ljungdahl, L.G.3    Kurtz Jr., D.M.4
  • 192
    • 70350200851 scopus 로고    scopus 로고
    • Multiple antioxidant proteins protect Chlorobaculum tepidum against oxygen and reactive oxygen species
    • H. Li, S. Jubelirer, A.M. Garcia Costas, N.U. Frigaard, and D.A. Bryant Multiple antioxidant proteins protect Chlorobaculum tepidum against oxygen and reactive oxygen species Arch. Microbiol. 191 2009 853 867
    • (2009) Arch. Microbiol. , vol.191 , pp. 853-867
    • Li, H.1    Jubelirer, S.2    Garcia Costas, A.M.3    Frigaard, N.U.4    Bryant, D.A.5
  • 193
    • 0035519262 scopus 로고    scopus 로고
    • Comparative genomics and bioenergetics
    • DOI 10.1016/S0005-2728(01)00227-4, PII S0005272801002274
    • J. Castresana Comparative genomics and bioenergetics Biochim. Biophys. Acta 1506 2001 147 162 (Pubitemid 34075225)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1506 , Issue.3 , pp. 147-162
    • Castresana, J.1
  • 194
    • 33748115102 scopus 로고    scopus 로고
    • Asymmetrical evolution of cytochrome bd subunits
    • W. Hao, and G.B. Golding Asymmetrical evolution of cytochrome bd subunits J. Mol. Evol. 62 2006 132 142
    • (2006) J. Mol. Evol. , vol.62 , pp. 132-142
    • Hao, W.1    Golding, G.B.2
  • 195
    • 56749160385 scopus 로고    scopus 로고
    • Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo
    • T. Lenn, M.C. Leake, and C.W. Mullineaux Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo Mol. Microbiol. 70 2008 1397 1407
    • (2008) Mol. Microbiol. , vol.70 , pp. 1397-1407
    • Lenn, T.1    Leake, M.C.2    Mullineaux, C.W.3
  • 196
    • 53849112638 scopus 로고    scopus 로고
    • Are Escherichia coli OXPHOS complexes concentrated in specialized zones within the plasma membrane?
    • T. Lenn, M.C. Leake, and C.W. Mullineaux Are Escherichia coli OXPHOS complexes concentrated in specialized zones within the plasma membrane? Biochem. Soc. Trans. 36 2008 1032 1036
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1032-1036
    • Lenn, T.1    Leake, M.C.2    Mullineaux, C.W.3
  • 198
    • 0032559025 scopus 로고    scopus 로고
    • Quinol and cytochrome oxidases in the cyanobacterium Synechocystis sp. PCC 6803
    • DOI 10.1021/bi981486n
    • C.A. Howitt, and W.F. Vermaas Quinol and cytochrome oxidases in the cyanobacterium Synechocystis sp. PCC 6803 Biochemistry 37 1998 17944 17951 (Pubitemid 29023950)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 17944-17951
    • Howitt, C.A.1    Vermaas, W.F.J.2
  • 200
    • 0035949438 scopus 로고    scopus 로고
    • Characterization of three bioenergetically active respiratory terminal oxidases in the cyanobacterium Synechocystis sp. strain PCC 6803
    • DOI 10.1016/S0378-1097(01)00356-1, PII S0378109701003561
    • D. Pils, and G. Schmetterer Characterization of three bioenergetically active respiratory terminal oxidases in the cyanobacterium Synechocystis sp. strain PCC 6803 FEMS Microbiol. Lett. 203 2001 217 222 (Pubitemid 32913618)
    • (2001) FEMS Microbiology Letters , vol.203 , Issue.2 , pp. 217-222
    • Pils, D.1    Schmetterer, G.2
  • 201
    • 0037066090 scopus 로고    scopus 로고
    • Electron transport routes in whole cells of Synechocystis sp. Strain PCC 6803: The role of the cytochrome bd-type oxidase
    • DOI 10.1021/bi011683d
    • S. Berry, D. Schneider, W.F. Vermaas, and M. Rogner Electron transport routes in whole cells of Synechocystis sp. strain PCC 6803: the role of the cytochrome bd-type oxidase Biochemistry 41 2002 3422 3429 (Pubitemid 34214041)
    • (2002) Biochemistry , vol.41 , Issue.10 , pp. 3422-3429
    • Berry, S.1    Schneider, D.2    Vermaas, W.F.J.3    Rogner, M.4
  • 202
    • 7044253606 scopus 로고    scopus 로고
    • Respiratory terminal oxidases in the facultative chemoheterotrophic and dinitrogen fixing cyanobacterium Anabaena variabilis strain ATCC 29413: Characterization of the cox2 locus
    • DOI 10.1016/j.bbabio.2004.06.009, PII S0005272804002221
    • D. Pils, C. Wilken, A. Valladares, E. Flores, and G. Schmetterer Respiratory terminal oxidases in the facultative chemoheterotrophic and dinitrogen fixing cyanobacterium Anabaena variabilis strain ATCC 29413: characterization of the cox2 locus Biochim. Biophys. Acta 1659 2004 32 45 (Pubitemid 39423605)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1659 , Issue.1 , pp. 32-45
    • Pils, D.1    Wilken, C.2    Valladares, A.3    Flores, E.4    Schmetterer, G.5
  • 204
    • 0242410314 scopus 로고    scopus 로고
    • Photosynthetic and respiratory electron transport in the alkaliphilic cyanobacterium Arthrospira (Spirulina) platensis
    • DOI 10.1023/A:1026012719612
    • S. Berry, Y.V. Bolychevtseva, M. Rogner, and N.V. Karapetyan Photosynthetic and respiratory electron transport in the alkaliphilic cyanobacterium Arthrospira (Spirulina) platensis Photosynth. Res. 78 2003 67 76 (Pubitemid 37365230)
    • (2003) Photosynthesis Research , vol.78 , Issue.1 , pp. 67-76
    • Berry, S.1    Bolychevtseva, Y.V.2    Rogner, M.3    Karapetyan, N.V.4
  • 205
    • 32444448292 scopus 로고    scopus 로고
    • Sll1717 affects the redox state of the plastoquinone pool by modulating quinol oxidase activity in thylakoids
    • DOI 10.1128/JB.188.4.1286-1294.2006
    • G.I. Kufryk, and W.F. Vermaas Sll1717 affects the redox state of the plastoquinone pool by modulating quinol oxidase activity in thylakoids J. Bacteriol. 188 2006 1286 1294 (Pubitemid 43228661)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1286-1294
    • Kufryk, G.I.1    Vermaas, W.F.J.2
  • 206
    • 33847137761 scopus 로고    scopus 로고
    • Inhibition of respiration and nitrate assimilation enhances photohydrogen evolution under low oxygen concentrations in Synechocystis sp. PCC 6803
    • DOI 10.1016/j.bbabio.2006.12.003, PII S0005272806003690
    • F. Gutthann, M. Egert, A. Marques, and J. Appel Inhibition of respiration and nitrate assimilation enhances photohydrogen evolution under low oxygen concentrations in Synechocystis sp. PCC 6803 Biochim. Biophys. Acta 1767 2007 161 169 (Pubitemid 46282607)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.2 , pp. 161-169
    • Gutthann, F.1    Egert, M.2    Marques, A.3    Appel, J.4
  • 207
    • 70350454746 scopus 로고    scopus 로고
    • Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803
    • Y. Tsunoyama, G. Bernat, N.G. Dyczmons, D. Schneider, and M. Rogner Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803 J. Biol. Chem. 284 2009 27875 27883
    • (2009) J. Biol. Chem. , vol.284 , pp. 27875-27883
    • Tsunoyama, Y.1    Bernat, G.2    Dyczmons, N.G.3    Schneider, D.4    Rogner, M.5
  • 208
    • 0029091118 scopus 로고
    • Occurrence of heme O in photoheterotrophically growing, semi-anaerobic cyanobacterium Synechocystis sp. PCC6803
    • G.A. Peschek, M. Wastyn, S. Fromwald, and B. Mayer Occurrence of heme O in photoheterotrophically growing, semi-anaerobic cyanobacterium Synechocystis sp. PCC6803 FEBS Lett. 371 1995 89 93
    • (1995) FEBS Lett. , vol.371 , pp. 89-93
    • Peschek, G.A.1    Wastyn, M.2    Fromwald, S.3    Mayer, B.4
  • 209
    • 0033167113 scopus 로고    scopus 로고
    • Extended heme promiscuity in the cyanobacterial cytochrome c oxidase: Characterization of native complexes containing hemes A, O, and D, respectively
    • DOI 10.1006/abbi.1999.1236
    • S. Fromwald, R. Zoder, M. Wastyn, M. Lubben, and G.A. Peschek Extended heme promiscuity in the cyanobacterial cytochrome c oxidase: characterization of native complexes containing hemes A, O, and D, respectively Arch. Biochem. Biophys. 367 1999 122 128 (Pubitemid 29394201)
    • (1999) Archives of Biochemistry and Biophysics , vol.367 , Issue.1 , pp. 122-128
    • Fromwald, S.1    Zoder, R.2    Wastyn, M.3    Lubben, M.4    Peschek, G.A.5
  • 210
    • 1542648853 scopus 로고    scopus 로고
    • The respiratory chain of blue-green algae (cyanobacteria)
    • DOI 10.1111/j.1399-3054.2004.00274.x
    • G.A. Peschek, C. Obinger, and M. Paumann The respiratory chain of blue-green algae (cyanobacteria) Physiol. Plant. 120 2004 358 369 (Pubitemid 38335123)
    • (2004) Physiologia Plantarum , vol.120 , Issue.3 , pp. 358-369
    • Peschek, G.A.1    Obinger, C.2    Paumann, M.3
  • 212
    • 0037046156 scopus 로고    scopus 로고
    • FTIR spectroscopic evidence for the involvement of an acidic residue in quinone binding in cytochrome bd from Escherichia coli
    • DOI 10.1021/bi011784b
    • J. Zhang, W. Oettmeier, R.B. Gennis, and P. Hellwig FTIR spectroscopic evidence for the involvement of an acidic residue in quinone binding in cytochrome bd from Escherichia coli Biochemistry 41 2002 4612 4617 (Pubitemid 34275662)
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4612-4617
    • Zhang, J.1    Oettmeier, W.2    Gennis, R.B.3    Hellwig, P.4
  • 216
    • 0030049873 scopus 로고    scopus 로고
    • A study of the stabilization of semiquinones by the Escherichia coli quinol oxidase cytochrome bd
    • S.F. Hastings, and W.J. Ingledew A study of the stabilization of semiquinones by the Escherichia coli quinol oxidase cytochrome bd Biochem. Soc. Trans. 24 1996 131 132 (Pubitemid 26052386)
    • (1996) Biochemical Society Transactions , vol.24 , Issue.1 , pp. 131-132
    • Hastings, S.F.1    Ingledew, W.J.2
  • 217
    • 0032127499 scopus 로고    scopus 로고
    • Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli
    • S.F. Hastings, T.M. Kaysser, F. Jiang, J.C. Salerno, R.B. Gennis, and W.J. Ingledew Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli Eur. J. Biochem. 255 1998 317 323 (Pubitemid 28316868)
    • (1998) European Journal of Biochemistry , vol.255 , Issue.1 , pp. 317-323
    • Hastings, S.F.1    Kaysser, T.M.2    Jiang, F.3    Salerno, J.C.4    Gennis, R.B.5    Ingledew, W.J.6
  • 218
    • 17144445848 scopus 로고
    • The respiratory chain of anaerobically grown Escherichia coli: Reactions with nitrite and oxygen
    • R.A. Rothery, A.M. Houston, and W.J. Ingledew The respiratory chain of anaerobically grown Escherichia coli: Reactions with nitrite and oxygen J. Gen. Microbiol. 133 1987 3247 3255
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 3247-3255
    • Rothery, R.A.1    Houston, A.M.2    Ingledew, W.J.3
  • 219
    • 0024976978 scopus 로고
    • EPR studies of the cytochrome-d complex of Escherichia coli
    • S.W. Meinhardt, R.B. Gennis, and T. Ohnishi EPR studies of the cytochrome-d complex of Escherichia coli Biochim. Biophys. Acta 975 1989 175 184
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 175-184
    • Meinhardt, S.W.1    Gennis, R.B.2    Ohnishi, T.3
  • 220
    • 0024348253 scopus 로고
    • The cytochromes of anaerobically grown Escherichia coli
    • R. Rothery, and W.J. Ingledew The cytochromes of anaerobically grown Escherichia coli Biochem. J. 262 1989 437 443
    • (1989) Biochem. J. , vol.262 , pp. 437-443
    • Rothery, R.1    Ingledew, W.J.2
  • 221
    • 0026337648 scopus 로고
    • Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by Resonance Raman spectrosopy
    • M.A. Kahlow, T.M. Zuberi, R.B. Gennis, and T.M. Loehr Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by Resonance Raman spectrosopy Biochemistry 30 1991 11485 11489
    • (1991) Biochemistry , vol.30 , pp. 11485-11489
    • Kahlow, M.A.1    Zuberi, T.M.2    Gennis, R.B.3    Loehr, T.M.4
  • 222
    • 0028625501 scopus 로고
    • The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli
    • B.C. Hill, J.J. Hill, and R.B. Gennis The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli Biochemistry 33 1994 15110 15115
    • (1994) Biochemistry , vol.33 , pp. 15110-15115
    • Hill, B.C.1    Hill, J.J.2    Gennis, R.B.3
  • 223
    • 0026580478 scopus 로고
    • The orientation of the three haems of the in situ ubiquinol oxidase, cytochrome bd, of Escherichia coli
    • W.J. Ingledew, R.A. Rothery, R.B. Gennis, and J.C. Salerno The orientation of the three haems of the in situ ubiquinol oxidase, cytochrome bd, of Escherichia coli Biochem. J. 282 1992 255 259
    • (1992) Biochem. J. , vol.282 , pp. 255-259
    • Ingledew, W.J.1    Rothery, R.A.2    Gennis, R.B.3    Salerno, J.C.4
  • 224
    • 0000370757 scopus 로고
    • Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli
    • J.G. Koland, M.J. Miller, and R.B. Gennis Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli Biochemistry 23 1984 1051 1056
    • (1984) Biochemistry , vol.23 , pp. 1051-1056
    • Koland, J.G.1    Miller, M.J.2    Gennis, R.B.3
  • 225
    • 67649998728 scopus 로고    scopus 로고
    • Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli
    • D.A. Bloch, V.B. Borisov, T. Mogi, and M.I. Verkhovsky Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli Biochim. Biophys. Acta 1787 2009 1246 1253
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1246-1253
    • Bloch, D.A.1    Borisov, V.B.2    Mogi, T.3    Verkhovsky, M.I.4
  • 226
    • 0024411033 scopus 로고
    • Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis
    • H. Fang, R.-J. Lin, and R.B. Gennis Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis J. Biol. Chem. 264 1989 8026 8032 (Pubitemid 19137284)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.14 , pp. 8026-8032
    • Fang, H.1    Lin, R.-J.2    Gennis, R.B.3
  • 229
    • 1542346467 scopus 로고    scopus 로고
    • 2 reactive site near the periplasmic surface
    • DOI 10.1016/S0014-5793(04)00125-5, PII S0014579304001255
    • 2 reactive site near the periplasmic surface FEBS Lett. 561 2004 58 62 (Pubitemid 38324607)
    • (2004) FEBS Letters , vol.561 , Issue.1-3 , pp. 58-62
    • Zhang, J.1    Barquera, B.2    Gennis, R.B.3
  • 231
    • 0007452186 scopus 로고
    • Interaction of cytochrome bd from Escherichia coli with hydrogen peroxide
    • (translated from Biokhimiya (in Russian) (1995), 60, 315-327)
    • V.B. Borisov, R.B. Gennis, and A.A. Konstantinov Interaction of cytochrome bd from Escherichia coli with hydrogen peroxide Biochemistry (Moscow) 60 1995 231 239 (translated from Biokhimiya (in Russian) (1995), 60, 315-327)
    • (1995) Biochemistry (Moscow) , vol.60 , pp. 231-239
    • Borisov, V.B.1    Gennis, R.B.2    Konstantinov, A.A.3
  • 232
    • 0023648080 scopus 로고
    • 1-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d
    • 1-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d FEBS Lett. 217 1987 49 52
    • (1987) FEBS Lett. , vol.217 , pp. 49-52
    • Poole, R.K.1    Williams, H.D.2
  • 233
    • 0023650036 scopus 로고
    • Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli
    • A. Hata-Tanaka, K. Matsuura, S. Itoh, and Y. Anraku Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli Biochim. Biophys. Acta 893 1987 289 295
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 289-295
    • Hata-Tanaka, A.1    Matsuura, K.2    Itoh, S.3    Anraku, Y.4
  • 234
    • 0029981912 scopus 로고    scopus 로고
    • The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: Implications for regulation of activity in vivo by oxygen inhibition
    • R. D'mello, S. Hill, and R.K. Poole The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two-oxygen-binding haems: implicaitons for regulation of activity in vivo by oxygen inihibition Microbiology 142 1996 755 763 (Pubitemid 26139350)
    • (1996) Microbiology , vol.142 , Issue.4 , pp. 755-763
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 235
    • 33845378891 scopus 로고
    • Proposed structure of heme d, a prosthetic group of bacterial terminal oxidases
    • R. Timkovich, M.S. Cork, R.B. Gennis, and P.Y. Johnson Proposed structure of heme d, a prosthetic group of bacterial terminal oxidases J. Am. Chem. Soc. 107 1985 6069 6075
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6069-6075
    • Timkovich, R.1    Cork, M.S.2    Gennis, R.B.3    Johnson, P.Y.4
  • 236
    • 0020627779 scopus 로고
    • The 650 nm chromophore in Escherichia coli is an 'oxy'- or oxygenated compound, not the oxidized form of cytochrome oxidase d: An hypothesis
    • R.K. Poole, C. Kumar, I. Salmon, and B. Chance The 650 nm chromophore in Escherichia coli is an 'Oxy-' or oxygenated compound, not the oxidized form of cytochrome oxidase d: a hypothesis J. Gen. Microbiol. 129 1983 1335 1344 (Pubitemid 13094096)
    • (1983) Journal of General Microbiology , vol.129 , Issue.5 , pp. 1335-1344
    • Poole, R.K.1    Kumar, C.2    Salmon, I.3    Chance, B.4
  • 237
    • 0024603308 scopus 로고
    • Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli
    • R.M. Lorence, and R.B. Gennis Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli J. Biol. Chem. 264 1989 7135 7140 (Pubitemid 19119122)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7135-7140
    • Lorence, R.M.1    Gennis, R.B.2
  • 239
    • 0038865077 scopus 로고
    • Oxygenated cytochrome bd from Escherichia coli can be converted into the oxidized form by lipophilic electron acceptors
    • (translated from Biokhimiya (in Russian) (1994), 59, 598-606)
    • V.B. Borisov, I.A. Smirnova, I.A. Krasnosel'skaya, and A.A. Konstantinov Oxygenated cytochrome bd from Escherichia coli can be converted into the oxidized form by lipophilic electron acceptors Biochemistry (Moscow) 59 1994 437 443 (translated from Biokhimiya (in Russian) (1994), 59, 598-606)
    • (1994) Biochemistry (Moscow) , vol.59 , pp. 437-443
    • Borisov, V.B.1    Smirnova, I.A.2    Krasnosel'Skaya, I.A.3    Konstantinov, A.A.4
  • 240
    • 24044519364 scopus 로고    scopus 로고
    • Oxygenated complex of cytochrome bd from Escherichia coli: Stability and photolability
    • DOI 10.1016/j.febslet.2005.07.011, PII S0014579305008549
    • I. Belevich, V.B. Borisov, A.A. Konstantinov, and M.I. Verkhovsky Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability FEBS Lett. 579 2005 4567 4570 (Pubitemid 41218628)
    • (2005) FEBS Letters , vol.579 , Issue.21 , pp. 4567-4570
    • Belevich, I.1    Borisov, V.B.2    Konstantinov, A.A.3    Verkhovsky, M.I.4
  • 241
    • 34848914107 scopus 로고    scopus 로고
    • Cytochrome bd from Azotobacter vinelandii: Evidence for high-affinity oxygen binding
    • DOI 10.1021/bi700862u
    • I. Belevich, V.B. Borisov, D.A. Bloch, A.A. Konstantinov, and M.I. Verkhovsky Cytochrome bd from Azotobacter vinelandii: evidence for high-affinity oxygen binding Biochemistry 46 2007 11177 11184 (Pubitemid 47502783)
    • (2007) Biochemistry , vol.46 , Issue.39 , pp. 11177-11184
    • Belevich, I.1    Borisov, V.B.2    Bloch, D.A.3    Konstantinov, A.A.4    Verkhovsky, M.I.5
  • 242
    • 0030809827 scopus 로고    scopus 로고
    • Spontaneous spectral changes of the reduced cytochrome bd
    • DOI 10.1016/S0014-5793(97)01196-4, PII S0014579397011964
    • N. Azarkina, V. Borisov, and A.A. Konstantinov Spontaneous spectral changes of the reduced cytochrome bd FEBS Lett. 416 1997 171 174 (Pubitemid 27462781)
    • (1997) FEBS Letters , vol.416 , Issue.2 , pp. 171-174
    • Azarkina, N.1    Borisov, V.2    Konstantinov, A.A.3
  • 244
    • 84984233402 scopus 로고
    • Resonance Raman study on axial ligands of heme irons in cytochrome bd-type ubiquinol oxidase from Escherichia coli
    • S. Hirota, T. Mogi, Y. Anraku, R.B. Gennis, and T. Kitagawa Resonance Raman study on axial ligands of heme irons in cytochrome bd-type ubiquinol oxidase from Escherichia coli Biospectroscopy 1 1995 305 311
    • (1995) Biospectroscopy , vol.1 , pp. 305-311
    • Hirota, S.1    Mogi, T.2    Anraku, Y.3    Gennis, R.B.4    Kitagawa, T.5
  • 245
    • 0029942493 scopus 로고    scopus 로고
    • EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli
    • H. Hori, M. Tsubaki, T. Mogi, and Y. Anraku EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli J. Biol. Chem. 271 1996 9254 9258
    • (1996) J. Biol. Chem. , vol.271 , pp. 9254-9258
    • Hori, H.1    Tsubaki, M.2    Mogi, T.3    Anraku, Y.4
  • 246
    • 67651155844 scopus 로고    scopus 로고
    • Probing the heme d-binding site in cytochrome bd quinol oxidase by site-directed mutagenesis
    • T. Mogi Probing the heme d-binding site in cytochrome bd quinol oxidase by site-directed mutagenesis J. Biochem. 145 2009 763 770
    • (2009) J. Biochem. , vol.145 , pp. 763-770
    • Mogi, T.1
  • 247
    • 0017175074 scopus 로고
    • Redox potentials of the cytochromes in the respiratory chain of aerobically grown Escherichia coli
    • M.R. Pudek, and P.D. Bragg Redox potentials of the cytochromes in the respiratory chain of aerobically grown Escherichia coli Arch. Biochem. Biophys. 174 1976 546 552
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 546-552
    • Pudek, M.R.1    Bragg, P.D.2
  • 248
    • 0021769529 scopus 로고
    • Effects of pH and detergent on the kinetic and electrochemical properties of the purified cytochrome d terminal oxidase complex of Escherichia coli
    • R.M. Lorence, M.J. Miller, A. Borochov, R. Faiman-Weinberg, and R.B. Gennis Effects of pH and detergent on the kinetic and electrochemical properties of the purified cytochrome d terminal oxidase complex of Escherichia coli Biochim. Biophys. Acta 790 1984 148 153
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 148-153
    • Lorence, R.M.1    Miller, M.J.2    Borochov, A.3    Faiman-Weinberg, R.4    Gennis, R.B.5
  • 249
    • 0041148170 scopus 로고    scopus 로고
    • Effects of decyl-aurachin D and reversed electron transfer in cytochrome bd
    • DOI 10.1021/bi970055m
    • S. Jünemann, J.M. Wrigglesworth, and P.R. Rich Effects of decyl-aurachin D and reversed electron transfer in cytochrome bd Biochemistry 36 1997 9323 9331 (Pubitemid 27346969)
    • (1997) Biochemistry , vol.36 , Issue.31 , pp. 9323-9331
    • Junemann, S.1    Wrigglesworth, J.M.2    Rich, P.R.3
  • 251
    • 0031992408 scopus 로고    scopus 로고
    • Participation of the bacterial respiratory chain in tellurite reduction
    • S.M. Trutko, N.E. Suzina, V.I. Duda, V.K. Akimenko, and A.M. Boronin Participation of the bacterial respiratory chain in reduction of potassium tellurite Dokl. Akad. Nauk (in Russian) 358 1998 836 838 (Pubitemid 128763812)
    • (1998) Doklady Akademii Nauk , vol.358 , Issue.6 , pp. 836-838
    • Trutko, S.M.1    Suzina, N.E.2    Duda, V.I.3    Akimenko, V.K.4    Boronin, A.M.5
  • 252
    • 33745641297 scopus 로고    scopus 로고
    • Kinetic mechanism of quinol oxidation by cytochrome bd studied with ubiquinone-2 analogs
    • DOI 10.1093/jb/mvj087
    • Y. Matsumoto, E. Muneyuki, D. Fujita, K. Sakamoto, H. Miyoshi, M. Yoshida, and T. Mogi Kinetic mechanism of quinol oxidation by cytochrome bd studied with ubiquinone-2 analogs J. Biochem. (Tokyo) 139 2006 779 788 (Pubitemid 43973925)
    • (2006) Journal of Biochemistry , vol.139 , Issue.4 , pp. 779-788
    • Matsumoto, Y.1    Muneyuki, E.2    Fujita, D.3    Sakamoto, K.4    Miyoshi, H.5    Yoshida, M.6    Moggi, T.7
  • 253
    • 11144227980 scopus 로고    scopus 로고
    • Arginine 391 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli stabilizes the reduced form of the hemes and is essential for quinol oxidase activity
    • DOI 10.1074/jbc.M408626200
    • J. Zhang, P. Hellwig, J.P. Osborne, and R.B. Gennis Arginine 391 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli stabilizes the reduced form of the hemes and is essential for quinol oxidase activity J. Biol. Chem. 279 2004 53980 53987 (Pubitemid 40053129)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 53980-53987
    • Zhang, J.1    Hellwig, P.2    Osborne, J.P.3    Gennis, R.B.4
  • 254
    • 0026009165 scopus 로고
    • Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli
    • K.L. Oden, and R.B. Gennis Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli J. Bacteriol. 173 1991 6174 6183
    • (1991) J. Bacteriol. , vol.173 , pp. 6174-6183
    • Oden, K.L.1    Gennis, R.B.2
  • 255
    • 43249108452 scopus 로고    scopus 로고
    • Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: Heme d binds CO with high affinity
    • DOI 10.1007/s10541-008-1002-4
    • V.B. Borisov Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity Biochemistry (Moscow) 73 2008 14 22 (translated from Biokhimiya (in Russian) (2008), 73, 18-28) (Pubitemid 351653318)
    • (2008) Biochemistry (Moscow) , vol.73 , Issue.1 , pp. 14-22
    • Borisov, V.B.1
  • 256
    • 0027730609 scopus 로고
    • Stoichiometry of CO binding to the cytochrome bd complex of Azotobacter vinelandii
    • S. Jünemann, and J.M. Wrigglesworth Stoichiometry of CO binding to the cytochrome bd complex of Azotobacter vinelandii Biochem. Soc. Trans. 21 1993 345S (Pubitemid 24011574)
    • (1993) Biochemical Society Transactions , vol.21 , Issue.4
    • Junemann, S.1    Wrigglesworth, J.M.2
  • 257
    • 0029062502 scopus 로고
    • Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site
    • S. Jünemann, and J.M. Wrigglesworth Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site J. Biol. Chem. 270 1995 16213 16220
    • (1995) J. Biol. Chem. , vol.270 , pp. 16213-16220
    • Jünemann, S.1    Wrigglesworth, J.M.2
  • 258
    • 0027248937 scopus 로고
    • +-motive oxidases of the o-type from Bacillus FTU and of the d-type from Escherichia coli
    • DOI 10.1016/0014-5793(93)81018-U
    • +-motive oxidases of the o-type from Bacillus FTU and of the d-type from Escherichia coli FEBS Lett. 327 1993 347 350 (Pubitemid 23228581)
    • (1993) FEBS Letters , vol.327 , Issue.3 , pp. 347-350
    • Muntyan, M.S.1    Bloch, D.A.2    Drachev, L.A.3    Skulachev, V.P.4
  • 260
    • 0021101983 scopus 로고
    • Nitrite, but not silver, ions induce spectral changes in Escherichia coli cytochrome d
    • J.A.M. Hubbard, M.N. Hughes, and R.K. Poole Nitrite, but not silver, ions induce spectral changes in Escherichia coli cytochrome d FEBS Lett. 164 1983 241 243
    • (1983) FEBS Lett. , vol.164 , pp. 241-243
    • Hubbard, J.A.M.1    Hughes, M.N.2    Poole, R.K.3
  • 261
    • 80052746775 scopus 로고
    • R.K. Poole, C.S. Dow, Academic Press London
    • J.A.M. Hubbard, M.N. Hughes, and R.K. Poole R.K. Poole, C.S. Dow, 1985 Academic Press London 231 236
    • (1985) , pp. 231-236
    • Hubbard, J.A.M.1    Hughes, M.N.2    Poole, R.K.3
  • 262
    • 0026067189 scopus 로고
    • Kinetics of the reactions of trioxodinitrate and nitrite ions with cytochrome d in Escherichia coli
    • F.T. Bonner, M.N. Hughes, R.K. Poole, and R.I. Scott Kinetics of the reactions of trioxodinitrate and nitrite ions with cytochrome d in Escherichia coli Biochim. Biophys. Acta 1056 1991 133 138
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 133-138
    • Bonner, F.T.1    Hughes, M.N.2    Poole, R.K.3    Scott, R.I.4
  • 263
    • 0019174890 scopus 로고
    • Effect of ligands on cytochrome d from Azotobacter vinelandii
    • DOI 10.1007/BF00744688
    • H.F. Kauffman, B.F. van Gelder, and D.V. DerVartanian Effect of ligands on cytochrome d from Azotobacter vinelandii J. Bioenerg. Biomembr. 12 1980 265 276 (Pubitemid 11220315)
    • (1980) Journal of Bioenergetics and Biomembranes , vol.12 , Issue.3-4 , pp. 265-276
    • Kauffman, H.F.1    Van Gelder, B.F.2
  • 264
    • 0030052702 scopus 로고    scopus 로고
    • Binding of NO to the oxygen reaction site of cytochrome bd from Azotobacter vinelandii
    • S. Jünemann, and J.M. Wrigglesworth Binding of NO to the oxygen reaction site of cytochrome bd from Azotobacter vinelandii Biochem. Soc. Trans. 24 1996 38S
    • (1996) Biochem. Soc. Trans. , vol.24
    • Jünemann, S.1    Wrigglesworth, J.M.2
  • 266
    • 0027359220 scopus 로고
    • The gateway to the active site of heme-copper oxidases
    • DOI 10.1021/bi00096a002
    • D.D. Lemon, M.W. Calhoun, R.B. Gennis, and W.H. Woodruff The gateway to the active site of heme-copper oxidases Biochemistry 32 1993 11953 11956 (Pubitemid 23353630)
    • (1993) Biochemistry , vol.32 , Issue.45 , pp. 11953-11956
    • Lemon, D.D.1    Calhoun, M.W.2    Gennis, R.B.3    Woodruff, W.H.4
  • 267
    • 0015864129 scopus 로고
    • The respiratory chain of Azotobacter vinelandii. II. The effect of cyanide on cytochrome d
    • H.F. Kauffman, and B.F. Van Gelder The respiratory chain of Azotobacter vinelandii. II. The effect of cyanide on cytochrome d Biochim. Biophys. Acta 314 1973 276 283
    • (1973) Biochim. Biophys. Acta , vol.314 , pp. 276-283
    • Kauffman, H.F.1    Van Gelder, B.F.2
  • 268
    • 0015971228 scopus 로고
    • The respiratory chain of Azotobacter vinelandii. III. The effect of cyanide in the presence of substrates
    • H.F. Kauffman, and B.F. Van Gelder The respiratory chain of Azotobacter vinelandii. III. The effect of cyanide in the presence of substrates Biochim. Biophys. Acta 333 1974 218 227
    • (1974) Biochim. Biophys. Acta , vol.333 , pp. 218-227
    • Kauffman, H.F.1    Van Gelder, B.F.2
  • 269
    • 0016277302 scopus 로고
    • Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli
    • M.R. Pudek, and P.D. Bragg Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli Arch. Biochem. Biophys. 164 1974 682 693
    • (1974) Arch. Biochem. Biophys. , vol.164 , pp. 682-693
    • Pudek, M.R.1    Bragg, P.D.2
  • 270
    • 0016441572 scopus 로고
    • Reaction of cyanide with cytochrome d in respiratory particles from exponential phase Escherichia coli
    • M.R. Pudek, and P.D. Bragg Reaction of cyanide with cytochrome d in respiratory particles from exponential phase Escherichia coli FEBS Lett. 50 1975 111 113
    • (1975) FEBS Lett. , vol.50 , pp. 111-113
    • Pudek, M.R.1    Bragg, P.D.2
  • 272
  • 273
    • 0035796994 scopus 로고    scopus 로고
    • The binding of cyanide to cytochrome d in intact cells, spheroplasts, membrane fragments and solubilized enzyme from Salmonella typhimurium
    • E. Keyhani, and D. Minai-Tehrani The binding of cyanide to cytochrome d in intact cells, spheroplasts, membrane fragments and solubilized enzyme from Salmonella typhimurium Biochim. Biophys. Acta 1506 2001
    • (2001) Biochim. Biophys. Acta , vol.1506
    • Keyhani, E.1    Minai-Tehrani, D.2
  • 274
    • 0016584320 scopus 로고
    • EPR studies on cytochrome components in phosphorylating particles of Azotobacter vinelandii
    • H.F. Kauffman, D.V. DerVartanian, B.F. van Gelder, and J. Wampler EPR studies on cytochrome components in phosphorylating particles of Azotobacter vinelandii J. Bioenerg. 7 1975 215 222
    • (1975) J. Bioenerg. , vol.7 , pp. 215-222
    • Kauffman, H.F.1    Dervartanian, D.V.2    Van Gelder, B.F.3    Wampler, J.4
  • 275
    • 0029121227 scopus 로고
    • Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as- isolated" enzyme and characterization of the cyanide adduct
    • J. Sun, J.P. Osborne, M.A. Kahlow, T.M. Kaysser, R.B. Gennis, and T.M. Loehr Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as- isolated" enzyme and characterization of the cyanide adduct Biochemistry 34 1995 12144 12151
    • (1995) Biochemistry , vol.34 , pp. 12144-12151
    • Sun, J.1    Osborne, J.P.2    Kahlow, M.A.3    Kaysser, T.M.4    Gennis, R.B.5    Loehr, T.M.6
  • 276
    • 0024284194 scopus 로고
    • Formation of the 680-nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form
    • R.K. Poole, and H.D. Williams Formation of the 680-nm-absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form FEBS Lett. 231 1988 243 246
    • (1988) FEBS Lett. , vol.231 , pp. 243-246
    • Poole, R.K.1    Williams, H.D.2
  • 278
    • 0028818107 scopus 로고
    • A suggested mechanism for the catalytic cycle of cytochrome bd terminal oxidase based on kinetic analysis
    • S. Jünemann, P.J. Butterworth, and J.M. Wrigglesworth A suggested mechanism for the catalytic cycle of cytochrome bd terminal oxidase based on kinetic analysis Biochemistry 34 1995 14861 14867
    • (1995) Biochemistry , vol.34 , pp. 14861-14867
    • Jünemann, S.1    Butterworth, P.J.2    Wrigglesworth, J.M.3
  • 279
    • 0028304990 scopus 로고
    • Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol
    • DOI 10.1016/0014-5793(94)00372-6
    • S. Jünemann, and J.M. Wrigglesworth Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol FEBS Lett. 345 1994 198 202 (Pubitemid 24188924)
    • (1994) FEBS Letters , vol.345 , Issue.2-3 , pp. 198-202
    • Junemann, S.1    Wrigglesworth, J.M.2
  • 280
    • 0021774196 scopus 로고
    • Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase
    • J.G. Koland, M.J. Miller, and R.B. Gennis Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase Biochemistry 23 1984 445 453
    • (1984) Biochemistry , vol.23 , pp. 445-453
    • Koland, J.G.1    Miller, M.J.2    Gennis, R.B.3
  • 282
    • 0000825077 scopus 로고
    • Reactions of cytochrome oxidase with oxygen and carbon monoxide
    • Q. Gibson, and C. Greenwood Reactions of cytochrome oxidase with oxygen and carbon monoxide Biochem. J. 86 1963 541 555
    • (1963) Biochem. J. , vol.86 , pp. 541-555
    • Gibson, Q.1    Greenwood, C.2
  • 283
    • 79954853196 scopus 로고    scopus 로고
    • Catalytic intermediates of cytochrome bd terminal oxidase at steady-state: Ferryl and oxy-ferrous species dominate
    • V.B. Borisov, E. Forte, P. Sarti, and A. Giuffrè Catalytic intermediates of cytochrome bd terminal oxidase at steady-state: ferryl and oxy-ferrous species dominate Biochim. Biophys. Acta 1807 2011 503 509
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 503-509
    • Borisov, V.B.1    Forte, E.2    Sarti, P.3    Giuffrè, A.4
  • 284
    • 70149103333 scopus 로고    scopus 로고
    • The steady-state mechanism of cytochrome c oxidase: Redox interactions between metal centres
    • M.G. Mason, P. Nicholls, and C.E. Cooper The steady-state mechanism of cytochrome c oxidase: redox interactions between metal centres Biochem. J. 422 2009 237 246
    • (2009) Biochem. J. , vol.422 , pp. 237-246
    • Mason, M.G.1    Nicholls, P.2    Cooper, C.E.3
  • 285
    • 0028931296 scopus 로고
    • New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd
    • B. Meunier, S.A. Madgwick, E. Reil, W. Oettmeier, and P.R. Rich New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd Biochemistry 34 1995 1076 1083
    • (1995) Biochemistry , vol.34 , pp. 1076-1083
    • Meunier, B.1    Madgwick, S.A.2    Reil, E.3    Oettmeier, W.4    Rich, P.R.5
  • 286
    • 17644436492 scopus 로고
    • Inhibitors of electron transport in the cytochrome bd complex of
    • S. Jünemann, and J.M. Wrigglesworth Inhibitors of electron transport in the cytochrome bd complex of Azotobacter vinelandii Biochem. Soc. Trans. 22 1994 287S (Pubitemid 24272664)
    • (1994) Biochemical Society Transactions , vol.22 , Issue.3
    • Junemann, S.1    Wrigglesworth, J.M.2
  • 287
    • 0014194451 scopus 로고
    • The cytochrome system of Azotobacter vinelandii
    • C.W. Jones, and E.R. Redfearn The cytochrome system of Azotobacter vinelandii Biochim. Biophys. Acta 143 1967 340 353
    • (1967) Biochim. Biophys. Acta , vol.143 , pp. 340-353
    • Jones, C.W.1    Redfearn, E.R.2
  • 288
    • 0022573635 scopus 로고
    • 560-d complex, a terminal oxidase of the aerobic respiratory chain of Photobacterium phosphoreum
    • 560-d complex, a terminal oxidase of the aerobic respiratory chain of Photobacterium phosphoreum J. Biochem. 99 1986 1227 1236 (Pubitemid 16090607)
    • (1986) Journal of Biochemistry , vol.99 , Issue.4 , pp. 1227-1236
    • Konishi, K.1    Ouchi, M.2    Kita, K.3    Horikoshi, I.4
  • 289
    • 0031708947 scopus 로고    scopus 로고
    • Redox poise and oxygenation of cytochrome bd in the diazotroph Azotobacter vinelandii assessed in vivo using diode-array reflectance spectrophotometry
    • E.P. Kavanagh, J.B. Callis, S.E. Edwards, R.K. Poole, and S. Hill Redox poise and oxygenation of cytochrome bd in the diazotroph Azotobacter vinelandii assessed in vivo using diode-array reflectance spectrophotometry Microbiology 144 Pt 8 1998 2271 2280 (Pubitemid 28403041)
    • (1998) Microbiology , vol.144 , Issue.8 , pp. 2271-2280
    • Kavanagh, E.P.1    Callis, J.B.2    Edwards, S.E.3    Poole, R.K.4    Hill, S.5
  • 290
    • 53949095409 scopus 로고    scopus 로고
    • The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: Direct evidence from rapid kinetics studies
    • K. Yang, V.B. Borisov, A.A. Konstantinov, and R.B. Gennis The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: direct evidence from rapid kinetics studies FEBS Lett. 582 2008 3705 3709
    • (2008) FEBS Lett. , vol.582 , pp. 3705-3709
    • Yang, K.1    Borisov, V.B.2    Konstantinov, A.A.3    Gennis, R.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.