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Volumn 1847, Issue 2, 2015, Pages 182-188

Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition

Author keywords

Cytochrome bd; Escherichia coli; Immune response; Nitrosative and oxidative stress; Peroxynitrite; Reactive nitrogen species

Indexed keywords

ASCORBIC ACID; CYTOCHROME; CYTOCHROME BD; N,N,N',N' TETRAMETHYL 1,4 PHENYLENEDIAMINE; OXIDOREDUCTASE; OXYGEN; PEROXYNITRITE; UNCLASSIFIED DRUG; CYTOCHROME BD TERMINAL OXIDASE COMPLEX, E COLI; ESCHERICHIA COLI PROTEIN; MULTIENZYME COMPLEX; PEROXYNITROUS ACID;

EID: 84913554227     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.10.006     Document Type: Article
Times cited : (37)

References (71)
  • 1
    • 84884169659 scopus 로고    scopus 로고
    • Peroxynitrite, a stealthy biological oxidant
    • R. Radi, Peroxynitrite, a stealthy biological oxidant, J. Biol. Chem. 288 (2013) 26464-26472.
    • (2013) J. Biol. Chem. , vol.288 , pp. 26464-26472
    • Radi, R.1
  • 2
    • 84899092424 scopus 로고    scopus 로고
    • Peroxynitrite, a potent macrophage-derived oxidizing cytotoxin to combat invading pathogens
    • C. Prolo, M.N. Alvarez, R. Radi, Peroxynitrite, a potent macrophage-derived oxidizing cytotoxin to combat invading pathogens, Biofactors 40 (2014) 215-225.
    • (2014) Biofactors , vol.40 , pp. 215-225
    • Prolo, C.1    Alvarez, M.N.2    Radi, R.3
  • 3
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • P. Pacher, J.S. Beckman, L. Liaudet, Nitric oxide and peroxynitrite in health and disease, Physiol. Rev. 87 (2007) 315-424.
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 5
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • A. Cassina, R. Radi, Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport, Arch. Biochem. Biophys. 328 (1996) 309-316.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 6
    • 0035708661 scopus 로고    scopus 로고
    • Identification of respiratory complexes I and III asmitochondrial sites of damage following exposure to ionizing radiation and nitric oxide
    • L.L. Pearce, M.W. Epperly, J.S. Greenberger, B.R. Pitt, J. Peterson, Identification of respiratory complexes I and III asmitochondrial sites of damage following exposure to ionizing radiation and nitric oxide, Nitric Oxide 5 (2001) 128-136.
    • (2001) Nitric Oxide , vol.5 , pp. 128-136
    • Pearce, L.L.1    Epperly, M.W.2    Greenberger, J.S.3    Pitt, B.R.4    Peterson, J.5
  • 7
    • 0032553302 scopus 로고    scopus 로고
    • Interaction of peroxynitrite with mitochondrial cytochrome oxidase. Catalytic production of nitric oxide and irreversible inhibition of enzyme activity
    • M.A. Sharpe, C.E. Cooper, Interaction of peroxynitrite with mitochondrial cytochrome oxidase. Catalytic production of nitric oxide and irreversible inhibition of enzyme activity, J. Biol. Chem. 273 (1998) 30961-30972.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30961-30972
    • Sharpe, M.A.1    Cooper, C.E.2
  • 10
    • 42949116026 scopus 로고    scopus 로고
    • Nitric oxide irreversibly inhibits cytochrome oxidase at low oxygen concentrations: Evidence for inverse oxygen concentration-dependent peroxynitrite formation
    • A. Parihar, P. Vaccaro, P. Ghafourifar, Nitric oxide irreversibly inhibits cytochrome oxidase at low oxygen concentrations: evidence for inverse oxygen concentration-dependent peroxynitrite formation, IUBMB Life 60 (2008) 64-67.
    • (2008) IUBMB Life , vol.60 , pp. 64-67
    • Parihar, A.1    Vaccaro, P.2    Ghafourifar, P.3
  • 11
    • 0033928977 scopus 로고    scopus 로고
    • Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation
    • R.K. Poole, G.M. Cook, Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation, Adv. Microb. Physiol. 43 (2000) 165-224.
    • (2000) Adv. Microb. Physiol. , vol.43 , pp. 165-224
    • Poole, R.K.1    Cook, G.M.2
  • 12
    • 0030131933 scopus 로고    scopus 로고
    • Cytochrome bd: Structure and properties
    • V.B. Borisov, Cytochrome bd: structure and properties, Biochem. Mosc. 61 (1996) 565-574.
    • (1996) Biochem. Mosc. , vol.61 , pp. 565-574
    • Borisov, V.B.1
  • 13
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • S. Jünemann, Cytochrome bd terminal oxidase, Biochim. Biophys. Acta 1321 (1997) 107-127.
    • (1997) Biochim. Biophys. Acta , vol.1321 , pp. 107-127
    • Jünemann, S.1
  • 16
    • 0031559960 scopus 로고    scopus 로고
    • Generation of protonic potential by the bd-type quinol oxidase of Azotobacter vinelandii
    • Y.V. Bertsova, A.V. Bogachev, V.P. Skulachev, Generation of protonic potential by the bd-type quinol oxidase of Azotobacter vinelandii, FEBS Lett. 414 (1997) 369-372.
    • (1997) FEBS Lett. , vol.414 , pp. 369-372
    • Bertsova, Y.V.1    Bogachev, A.V.2    Skulachev, V.P.3
  • 18
    • 14844351539 scopus 로고    scopus 로고
    • Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site
    • I. Belevich, V.B. Borisov, J. Zhang, K. Yang, A.A. Konstantinov, R.B. Gennis, M.I. Verkhovsky, Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site, Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 3657-3662.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3657-3662
    • Belevich, I.1    Borisov, V.B.2    Zhang, J.3    Yang, K.4    Konstantinov, A.A.5    Gennis, R.B.6    Verkhovsky, M.I.7
  • 19
    • 35349019174 scopus 로고    scopus 로고
    • Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement
    • I. Belevich, V.B. Borisov, 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.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28514-28519
    • Belevich, I.1    Borisov, V.B.2    Verkhovsky, M.I.3
  • 22
    • 84868307693 scopus 로고    scopus 로고
    • Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth
    • P. Sharma, K.J. Hellingwerf, M.J. Teixeira de Mattos, M. Bekker, Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth, Appl. Environ. Microbiol. 78 (2012) 6908-6913.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 6908-6913
    • Sharma, P.1    Hellingwerf, K.J.2    Teixeira De Mattos, M.J.3    Bekker, M.4
  • 24
    • 84880988082 scopus 로고    scopus 로고
    • The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity
    • C.E. VanOrsdel, S. Bhatt, R.J. Allen, E.P. Brenner, J.J. Hobson, A. Jamil, B.M. Haynes, A.M. Genson, M.R. Hemm, The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity, J. Bacteriol. 195 (2013) 3640-3650.
    • (2013) J. Bacteriol. , vol.195 , pp. 3640-3650
    • VanOrsdel, C.E.1    Bhatt, S.2    Allen, R.J.3    Brenner, E.P.4    Hobson, J.J.5    Jamil, A.6    Haynes, B.M.7    Genson, A.M.8    Hemm, M.R.9
  • 25
    • 84899643926 scopus 로고    scopus 로고
    • Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site
    • J. Hoeser, S. Hong, G. Gehmann, R.B. Gennis, T. Friedrich, Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site, FEBS Lett. 588 (2014) 1537-1541.
    • (2014) FEBS Lett. , vol.588 , pp. 1537-1541
    • Hoeser, J.1    Hong, S.2    Gehmann, G.3    Gennis, R.B.4    Friedrich, T.5
  • 26
    • 0027299607 scopus 로고
    • Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
    • J.J. Hill, J.O. Alben, R.B. Gennis, Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli, Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 5863-5867.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5863-5867
    • Hill, J.J.1    Alben, J.O.2    Gennis, R.B.3
  • 27
    • 0028791167 scopus 로고
    • Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli
    • M. Tsubaki, H. Hori, T. Mogi, 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
  • 28
    • 0029554848 scopus 로고
    • Peroxide complex of cytochrome bd: Kinetics of generation and stability
    • V. Borisov, R. Gennis, A.A. Konstantinov, Peroxide complex of cytochrome bd: kinetics of generation and stability, Biochem. Mol. Biol. Int. 37 (1995) 975-982.
    • (1995) Biochem. Mol. Biol. Int. , vol.37 , pp. 975-982
    • Borisov, V.1    Gennis, R.2    Konstantinov, A.A.3
  • 29
    • 0007452186 scopus 로고
    • Interaction of cytochrome bd from Escherichia coli with hydrogen peroxide
    • V.B. Borisov, R.B. Gennis, A.A. Konstantinov, Interaction of cytochrome bd from Escherichia coli with hydrogen peroxide, Biochem. Mosc. 60 (1995) 231-239.
    • (1995) Biochem. Mosc. , vol.60 , pp. 231-239
    • Borisov, V.B.1    Gennis, R.B.2    Konstantinov, A.A.3
  • 30
    • 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, 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
  • 31
    • 0034652126 scopus 로고    scopus 로고
    • Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?
    • M.H. Vos, V.B. Borisov, U. Liebl, J.-L. Martin, A.A. Konstantinov, Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site? Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 1554-1559.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1554-1559
    • Vos, M.H.1    Borisov, V.B.2    Liebl, U.3    Martin, J.-L.4    Konstantinov, A.A.5
  • 35
    • 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, 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
  • 36
    • 84868244991 scopus 로고    scopus 로고
    • Accommodation of CO in the di-heme active site of cytochrome bd terminal oxidase from Escherichia coli
    • V.B. Borisov, M.I. Verkhovsky, Accommodation of CO in the di-heme active site of cytochrome bd terminal oxidase from Escherichia coli, J. Inorg. Biochem. 118 (2013) 65-67.
    • (2013) J. Inorg. Biochem. , vol.118 , pp. 65-67
    • Borisov, V.B.1    Verkhovsky, M.I.2
  • 37
    • 84899758882 scopus 로고    scopus 로고
    • Microsecond time-resolved absorption spectroscopy used to study CO compounds of cytochrome bd from Escherichia coli
    • S.A. Siletsky, A.A. Zaspa, R.K. Poole, V.B. Borisov, Microsecond time-resolved absorption spectroscopy used to study CO compounds of cytochrome bd from Escherichia coli, PLoS One 9 (2014) e95617 (doi:95610.91371/journal.pone.0095617).
    • (2014) PLoS One , vol.9 , pp. e95617
    • Siletsky, S.A.1    Zaspa, A.A.2    Poole, R.K.3    Borisov, V.B.4
  • 38
    • 0029062502 scopus 로고
    • Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site
    • S. Jünemann, 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
  • 39
    • 17144445848 scopus 로고
    • The respiratory chain of anaerobically grown Escherichia coli: Reactions with nitrite and oxygen
    • R.A. Rothery, A.M. Houston, 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
  • 40
    • 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, R.K. Poole, 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, Microbiology 142 (1996) 755-763.
    • (1996) Microbiology , vol.142 , pp. 755-763
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 41
    • 84857913190 scopus 로고    scopus 로고
    • Cytochrome bd oxidase and nitric oxide: From reaction mechanisms to bacterial physiology
    • A. Giuffrè, V.B. Borisov, D. Mastronicola, P. Sarti, E. Forte, Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology, FEBS Lett. 586 (2012) 622-629.
    • (2012) FEBS Lett. , vol.586 , pp. 622-629
    • Giuffrè, A.1    Borisov, V.B.2    Mastronicola, D.3    Sarti, P.4    Forte, E.5
  • 42
    • 84901845126 scopus 로고    scopus 로고
    • Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress
    • A. Giuffrè, V.B. Borisov, M. Arese, P. Sarti, E. Forte, Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress, Biochim. Biophys. Acta 1837 (2014) 1178-1187.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 1178-1187
    • Giuffrè, A.1    Borisov, V.B.2    Arese, M.3    Sarti, P.4    Forte, E.5
  • 43
    • 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, 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
  • 44
    • 0029917388 scopus 로고    scopus 로고
    • The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB strains are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents
    • B.S. Goldman, K.K. Gabbert, R.G. Kranz, The temperature-sensitive growth and survival phenotypes of Escherichia coli cydDC and cydAB strains are due to deficiencies in cytochrome bd and are corrected by exogenous catalase and reducing agents, J. Bacteriol. 178 (1996) 6348-6351.
    • (1996) J. Bacteriol. , vol.178 , pp. 6348-6351
    • Goldman, B.S.1    Gabbert, K.K.2    Kranz, R.G.3
  • 45
  • 46
    • 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
    • S.E. Edwards, C.S. Loder, G.Wu, H. Corker, B.W. Bainbridge, S. Hill, 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.
    • (2000) FEMS Microbiol. Lett. , vol.185 , 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
  • 47
    • 0035089129 scopus 로고    scopus 로고
    • Interruption of the cydB locus in Brucella abortus attenuates intracellular survival and virulence in the mouse model of infection
    • S. Endley, D. McMurray, 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.
    • (2001) J. Bacteriol. , vol.183 , pp. 2454-2462
    • Endley, S.1    McMurray, D.2    Ficht, T.A.3
  • 48
    • 77951684325 scopus 로고    scopus 로고
    • Peroxidase activity of cytochrome bd from Escherichia coli
    • V.B. Borisov, A.I. Davletshin, A.A. Konstantinov, Peroxidase activity of cytochrome bd from Escherichia coli, Biochem. Mosc. 75 (2010) 428-436.
    • (2010) Biochem. Mosc. , vol.75 , pp. 428-436
    • Borisov, V.B.1    Davletshin, A.I.2    Konstantinov, A.A.3
  • 49
    • 77949342990 scopus 로고    scopus 로고
    • Two sources of endogenous hydrogen peroxide in Escherichia coli
    • S. Korshunov, 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
  • 50
    • 84887201661 scopus 로고    scopus 로고
    • Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis
    • J.L. Small, S.W. Park, B.D. Kana, T.R. Ioerger, J.C. Sacchettini, S. Ehrt, Perturbation of cytochrome c maturation reveals adaptability of the respiratory chain in Mycobacterium tuberculosis, MBio 4 (2013) (e00475-00413).
    • (2013) MBio , vol.4 , pp. e00475-e100413
    • Small, J.L.1    Park, S.W.2    Kana, B.D.3    Ioerger, T.R.4    Sacchettini, J.C.5    Ehrt, S.6
  • 51
    • 84879688053 scopus 로고    scopus 로고
    • Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress
    • V.B. Borisov, E. Forte, A. Davletshin, D. Mastronicola, P. Sarti, A. Giuffrè, Cytochrome bd oxidase from Escherichia coli displays high catalase activity: an additional defense against oxidative stress, FEBS Lett. 587 (2013) 2214-2218.
    • (2013) FEBS Lett. , vol.587 , pp. 2214-2218
    • Borisov, V.B.1    Forte, E.2    Davletshin, A.3    Mastronicola, D.4    Sarti, P.5    Giuffrè, A.6
  • 52
    • 84891619410 scopus 로고    scopus 로고
    • Cytochrome bd oxidase and hydrogen peroxide resistance in Mycobacterium tuberculosis
    • E. Forte, V.B. Borisov, A. Davletshin, D. Mastronicola, P. Sarti, A. Giuffrè, Cytochrome bd oxidase and hydrogen peroxide resistance in Mycobacterium tuberculosis, MBio 4 (2013) e01006-e01013.
    • (2013) MBio , vol.4 , pp. e01006-e01013
    • Forte, E.1    Borisov, V.B.2    Davletshin, A.3    Mastronicola, D.4    Sarti, P.5    Giuffrè, A.6
  • 58
    • 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, 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
  • 59
    • 84883186311 scopus 로고    scopus 로고
    • Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or bo″ to inhibition by the carbon monoxide-releasing molecule, CORM-3: N-acetylcysteine reduces CORM uptake and inhibition of respiration
    • H.E. Jesse, T.L. Nye, S. McLean, J. Green, B.E. Mann, R.K. Poole, Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or bo″ to inhibition by the carbon monoxide-releasing molecule, CORM-3: N-acetylcysteine reduces CORM uptake and inhibition of respiration, Biochim. Biophys. Acta 1834 (2013) 1693-1703.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1693-1703
    • Jesse, H.E.1    Nye, T.L.2    McLean, S.3    Green, J.4    Mann, B.E.5    Poole, R.K.6
  • 60
    • 84881257026 scopus 로고    scopus 로고
    • Crp-dependent cytochrome bd oxidase confers nitrite resistance to Shewanella oneidensis
    • H. Fu, H. Chen, J. Wang, G. Zhou, H. Zhang, L. Zhang, H. Gao, Crp-dependent cytochrome bd oxidase confers nitrite resistance to Shewanella oneidensis, Environ. Microbiol. 15 (2013) 2198-2212.
    • (2013) Environ. Microbiol. , vol.15 , pp. 2198-2212
    • Fu, H.1    Chen, H.2    Wang, J.3    Zhou, G.4    Zhang, H.5    Zhang, L.6    Gao, H.7
  • 61
    • 84876550671 scopus 로고    scopus 로고
    • Impacts of nitrate and nitrite on physiology of Shewanella oneidensis
    • H. Zhang, H. Fu, J. Wang, L. Sun, Y. Jiang, L. Zhang, H. Gao, Impacts of nitrate and nitrite on physiology of Shewanella oneidensis, PLoS One 8 (2013) e62629.
    • (2013) PLoS One , vol.8 , pp. e62629
    • Zhang, H.1    Fu, H.2    Wang, J.3    Sun, L.4    Jiang, Y.5    Zhang, L.6    Gao, H.7
  • 62
    • 84888869356 scopus 로고    scopus 로고
    • Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Desulfovibrio vulgaris Hildenborough: Roles in oxygen defense and electron link with the periplasmic hydrogen oxidation
    • F. Ramel, A. Amrani, L. Pieulle, O. Lamrabet, G. Voordouw, N. Seddiki, D. Brethes, M. Company, A. Dolla, G. Brasseur, Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Desulfovibrio vulgaris Hildenborough: roles in oxygen defense and electron link with the periplasmic hydrogen oxidation, Microbiology 159 (2013) 2663-2673.
    • (2013) Microbiology , vol.159 , pp. 2663-2673
    • Ramel, F.1    Amrani, A.2    Pieulle, L.3    Lamrabet, O.4    Voordouw, G.5    Seddiki, N.6    Brethes, D.7    Company, M.8    Dolla, A.9    Brasseur, G.10
  • 63
    • 0022822121 scopus 로고
    • Purification and reconstitution of the cytochrome d terminal oxidase complex from Escherichia coli
    • M.J. Miller, R.B. Gennis, Purification and reconstitution of the cytochrome d terminal oxidase complex from Escherichia coli, Methods Enzymol. 126 (1986) 87-94.
    • (1986) Methods Enzymol. , vol.126 , pp. 87-94
    • Miller, M.J.1    Gennis, R.B.2
  • 64
    • 43249108452 scopus 로고    scopus 로고
    • Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: Heme d binds CO with high affinity
    • V.B. Borisov, Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity, Biochem. Mosc. 73 (2008) 14-22.
    • (2008) Biochem. Mosc. , vol.73 , pp. 14-22
    • Borisov, V.B.1
  • 66
    • 4544264011 scopus 로고    scopus 로고
    • Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols
    • M. Trujillo, H. Budde, M.D. Pineyro, M. Stehr, C. Robello, L. Flohe, R. Radi, Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols, J. Biol. Chem. 279 (2004) 34175-34182.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34175-34182
    • Trujillo, M.1    Budde, H.2    Pineyro, M.D.3    Stehr, M.4    Robello, C.5    Flohe, L.6    Radi, R.7
  • 67
    • 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, 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
  • 68
    • 0027184205 scopus 로고
    • Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: Comparison with enzymatically formed nitric oxide from L-arginine
    • L.J. Ignarro, J.M. Fukuto, J.M. Griscavage, N.E. Rogers, R.E. Byrns, Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: comparison with enzymatically formed nitric oxide from L-arginine, Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 8103-8107.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8103-8107
    • Ignarro, L.J.1    Fukuto, J.M.2    Griscavage, J.M.3    Rogers, N.E.4    Byrns, R.E.5
  • 69
    • 0034680875 scopus 로고    scopus 로고
    • Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo′ or bd, from nitric oxide
    • T.M. Stevanin, N. Ioannidis, C.E. Mills, S.O. Kim, M.N. Hughes, R.K. Poole, Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo′ or bd, from nitric oxide, J. Biol. Chem. 275 (2000) 35868-35875.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35868-35875
    • Stevanin, T.M.1    Ioannidis, N.2    Mills, C.E.3    Kim, S.O.4    Hughes, M.N.5    Poole, R.K.6
  • 71
    • 77954228805 scopus 로고    scopus 로고
    • Peroxynitrite toxicity in Escherichia coli K12 elicits expression of oxidative stress responses and protein nitration and nitrosylation
    • S. McLean, L.A. Bowman, G. Sanguinetti, R.C. Read, R.K. Poole, Peroxynitrite toxicity in Escherichia coli K12 elicits expression of oxidative stress responses and protein nitration and nitrosylation, J. Biol. Chem. 285 (2010) 20724-20731.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20724-20731
    • McLean, S.1    Bowman, L.A.2    Sanguinetti, G.3    Read, R.C.4    Poole, R.K.5


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