메뉴 건너뛰기




Volumn 1797, Issue 12, 2010, Pages 1924-1932

The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli

Author keywords

E. coli; EPR; Oxidase; Respiration; Ubiquinone

Indexed keywords

AMINO ACID; CYTOCHROME B; CYTOCHROME BO3 UBIQUINOL OXIDASE; OXIDOREDUCTASE; OXYGEN; QUINONE DERIVATIVE; SEMIQUINONE; UNCLASSIFIED DRUG;

EID: 78149467576     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.04.011     Document Type: Article
Times cited : (46)

References (48)
  • 1
    • 0031744093 scopus 로고    scopus 로고
    • Two terminal quinol oxidase families in Escherichia coli: variations on molecular machinery for dioxygen reduction
    • Mogi T., Tsubaki M., Hori H., Miyoshi H., Nakamura H., Anraku Y. Two terminal quinol oxidase families in Escherichia coli: variations on molecular machinery for dioxygen reduction. J. Biochem. Mol. Biol. Biophys. 1998, 2:79-110.
    • (1998) J. Biochem. Mol. Biol. Biophys. , vol.2 , pp. 79-110
    • Mogi, T.1    Tsubaki, M.2    Hori, H.3    Miyoshi, H.4    Nakamura, H.5    Anraku, Y.6
  • 2
    • 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
    • Cotter P.A., Gunsalus R.P. 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 Lett. 1992, 91:31-36.
    • (1992) FEMS Lett. , vol.91 , pp. 31-36
    • Cotter, P.A.1    Gunsalus, R.P.2
  • 3
    • 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
    • Tseng C.-P., Albrecht J., Gunsalus R.P. 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. Bact. 1996, 178:1094-1098.
    • (1996) J. Bact. , vol.178 , pp. 1094-1098
    • Tseng, C.-P.1    Albrecht, J.2    Gunsalus, R.P.3
  • 4
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evaluation of haem-copper oxygen reductases
    • Pereira M.M., Santana M., Teixeira M. A novel scenario for the evaluation of haem-copper oxygen reductases. Biochim. Biophys. Acta 2001, 1505:185-208.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 5
    • 44449146602 scopus 로고    scopus 로고
    • Diversity of the heme-copper superfamily in archaea: insights from genomics and structural modeling
    • Hemp J., Gennis R.B. Diversity of the heme-copper superfamily in archaea: insights from genomics and structural modeling. Results Probl. Cell Differ. 2008, 45:1-31.
    • (2008) Results Probl. Cell Differ. , vol.45 , pp. 1-31
    • Hemp, J.1    Gennis, R.B.2
  • 10
    • 0035818433 scopus 로고    scopus 로고
    • 3-600nm spectroscopic characterization of the steady-state species
    • 3-600nm spectroscopic characterization of the steady-state species. Biochemistry 2001, 40:13331-13341.
    • (2001) Biochemistry , vol.40 , pp. 13331-13341
    • Mattatall, N.R.1    Cameron, L.M.2    Hill, B.C.3
  • 11
    • 0027996364 scopus 로고
    • Identification of a novel quinone binding site in the cytochrome bo complex from Escherichia coli
    • Sato-Watanabe M., Mogi T., Ogura T., Kitagawa T., Miyoshi H., Iwamura H., Anraku Y. Identification of a novel quinone binding site in the cytochrome bo complex from Escherichia coli. J. Biol. Chem. 1994, 269:28908-28912.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28908-28912
    • Sato-Watanabe, M.1    Mogi, T.2    Ogura, T.3    Kitagawa, T.4    Miyoshi, H.5    Iwamura, H.6    Anraku, Y.7
  • 14
    • 0028143052 scopus 로고
    • Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenols
    • Sato-Watanabe M., Mogi T., Miyoshi H., Iwamura H., Matsushita K., Adachi O., Anraku Y. Structure-function studies on the ubiquinol oxidation site of the cytochrome bo complex from Escherichia coli using p-benzoquinones and substituted phenols. J. Biol. Chem. 1994, 269:28899-28907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28899-28907
    • Sato-Watanabe, M.1    Mogi, T.2    Miyoshi, H.3    Iwamura, H.4    Matsushita, K.5    Adachi, O.6    Anraku, Y.7
  • 15
    • 0029910353 scopus 로고    scopus 로고
    • Probing substrate binding site of the Escherichia coli quinol oxidases using synthetic ubiquinol analogues
    • Sakamoto K., Miyoshi H., Takegami K., Mogi T., Anraku Y., Iwamura H. Probing substrate binding site of the Escherichia coli quinol oxidases using synthetic ubiquinol analogues. J. Biol. Chem. 1996, 271:29897-29902.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29897-29902
    • Sakamoto, K.1    Miyoshi, H.2    Takegami, K.3    Mogi, T.4    Anraku, Y.5    Iwamura, H.6
  • 16
    • 0032573198 scopus 로고    scopus 로고
    • Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase
    • Sakamoto K., Miyoshi H., Ohshima M., Kuwabara K., Kano B., Akagi T., Mogi T., Iwamura H. Role of the isoprenyl tail of ubiquinone in reaction with respiratory enzymes: studies with bovine heart mitochondrial complex I and Escherichia coli bo-type ubiquinol oxidase. Biochemistry 1998, 37:15106-15113.
    • (1998) Biochemistry , vol.37 , pp. 15106-15113
    • Sakamoto, K.1    Miyoshi, H.2    Ohshima, M.3    Kuwabara, K.4    Kano, B.5    Akagi, T.6    Mogi, T.7    Iwamura, H.8
  • 18
    • 0028877684 scopus 로고
    • Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo
    • Ingledew W.J., Ohnishi T., Salerno J.C. Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo. Eur. J. Biochem. 1995, 227:903-908.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 903-908
    • Ingledew, W.J.1    Ohnishi, T.2    Salerno, J.C.3
  • 19
    • 0032765324 scopus 로고    scopus 로고
    • Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen
    • Mogi T., Sato-Watanabe M., Miyoshi H., Orii Y. Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen. FEBS Lett. 1999, 457:61-64.
    • (1999) FEBS Lett. , vol.457 , pp. 61-64
    • Mogi, T.1    Sato-Watanabe, M.2    Miyoshi, H.3    Orii, Y.4
  • 21
    • 0001704809 scopus 로고    scopus 로고
    • 3 with substoichiometric ubiquinol-2: a freeze-quench electron paramagnetic resonance investigation
    • 3 with substoichiometric ubiquinol-2: a freeze-quench electron paramagnetic resonance investigation. Biochemistry 1998, 37:4160-4168.
    • (1998) Biochemistry , vol.37 , pp. 4160-4168
    • Schultz, B.E.1    Edmondson, D.E.2    Chan, S.I.3
  • 22
    • 0034687655 scopus 로고    scopus 로고
    • Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo
    • Kobayashi K., Tagawea S., Mogi T. Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo. Biochemistry 2000, 39:15620-15625.
    • (2000) Biochemistry , vol.39 , pp. 15620-15625
    • Kobayashi, K.1    Tagawea, S.2    Mogi, T.3
  • 26
    • 0037183474 scopus 로고    scopus 로고
    • 3 from Escherichia coli by site-directed mutagenesis and EPR spectroscopy
    • 3 from Escherichia coli by site-directed mutagenesis and EPR spectroscopy. Biochemistry 2002, 41:10675-10679.
    • (2002) Biochemistry , vol.41 , pp. 10675-10679
    • Hellwig, P.1    Yano, T.2    Ohnishi, T.3    Gennis, R.B.4
  • 29
    • 0032530646 scopus 로고    scopus 로고
    • Isolation and characterizations of quinone analogue-resistant mutants of bo-type ubiquinol oxidase from Escherichia coli
    • Sato-Watanabe M., Mogi T., Sakamoto K., Miyoshi H., Anraku Y. Isolation and characterizations of quinone analogue-resistant mutants of bo-type ubiquinol oxidase from Escherichia coli. Biochemistry 1998, 37:12744-12752.
    • (1998) Biochemistry , vol.37 , pp. 12744-12752
    • Sato-Watanabe, M.1    Mogi, T.2    Sakamoto, K.3    Miyoshi, H.4    Anraku, Y.5
  • 34
    • 12544260148 scopus 로고    scopus 로고
    • Defining the Qp-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy
    • Rothery R.A., Seime A.M., Spiers A.M., Maklashina E., Schroder I., Gunsalus R.P., Cecchini G., Weiner J.H. Defining the Qp-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy. Febs J. 2005, 272:313-326.
    • (2005) Febs J. , vol.272 , pp. 313-326
    • Rothery, R.A.1    Seime, A.M.2    Spiers, A.M.3    Maklashina, E.4    Schroder, I.5    Gunsalus, R.P.6    Cecchini, G.7    Weiner, J.H.8
  • 35
    • 0033557414 scopus 로고    scopus 로고
    • Stopped-flow studies of the binding of 2-n-heptyl-4-hydroxyquinoline-N-oxide to fumarate reductase of Escherichia coli
    • Zhao Z., Rothery R.A., Weiner J.H. Stopped-flow studies of the binding of 2-n-heptyl-4-hydroxyquinoline-N-oxide to fumarate reductase of Escherichia coli. Eur. J. Biochem. 1999, 260:50-56.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 50-56
    • Zhao, Z.1    Rothery, R.A.2    Weiner, J.H.3
  • 36
    • 0032525923 scopus 로고    scopus 로고
    • Interaction of a menaquinol binding site with the [3Fe-4S] cluster of Escherichia coli fumarate reductase
    • Rothery R.A., Weiner J.H. Interaction of a menaquinol binding site with the [3Fe-4S] cluster of Escherichia coli fumarate reductase. Eur. J. Biochem. 1998, 254:588-595.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 588-595
    • Rothery, R.A.1    Weiner, J.H.2
  • 37
    • 0033613194 scopus 로고    scopus 로고
    • The hemes of Escherichia coli nitrate reductase A (NarGHI): potentiometric effects of inhibitor binding to narI
    • Rothery R.A., Blasco F., Magalon A., Asso M., Weiner J.H. The hemes of Escherichia coli nitrate reductase A (NarGHI): potentiometric effects of inhibitor binding to narI. Biochemistry 1999, 38:12747-12757.
    • (1999) Biochemistry , vol.38 , pp. 12747-12757
    • Rothery, R.A.1    Blasco, F.2    Magalon, A.3    Asso, M.4    Weiner, J.H.5
  • 38
    • 0035341125 scopus 로고    scopus 로고
    • L to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI)
    • L to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI). Biochemistry 2001, 40:5260-5268.
    • (2001) Biochemistry , vol.40 , pp. 5260-5268
    • Rothery, R.A.1    Blasco, F.2    Weiner, J.H.3
  • 39
    • 0032516875 scopus 로고    scopus 로고
    • Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli
    • Zhao Z., Weiner J.H. Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli. J. Biol. Chem. 1998, 273:20758-20763.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20758-20763
    • Zhao, Z.1    Weiner, J.H.2
  • 40
    • 0032974004 scopus 로고    scopus 로고
    • Characterization of the ubiquinol oxidation sites in cytochromes bo and bd from Escherichia coli using aurachin C. analogues
    • Miyoshi H., Takegami K., Sakamoto K., Mogi T., Iwamura H. Characterization of the ubiquinol oxidation sites in cytochromes bo and bd from Escherichia coli using aurachin C. analogues. J. Biochem. 1999, 125:138-142.
    • (1999) J. Biochem. , vol.125 , pp. 138-142
    • Miyoshi, H.1    Takegami, K.2    Sakamoto, K.3    Mogi, T.4    Iwamura, H.5
  • 41
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: function in the context of structure
    • 1 complex: function in the context of structure. Annu. Rev. Physiol. 2004, 66:689-733.
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 42
    • 0028931296 scopus 로고
    • New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd
    • Meunier B., Madgwick S.A., Reil E., Oettmeier W., Rich P.R. New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd. Biochemistry 1995, 34:1076-1083.
    • (1995) Biochemistry , vol.34 , pp. 1076-1083
    • Meunier, B.1    Madgwick, S.A.2    Reil, E.3    Oettmeier, W.4    Rich, P.R.5
  • 43
    • 0035969818 scopus 로고    scopus 로고
    • 3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy
    • 3-type ubiquinol oxidase studied by pulsed electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy. Biochemistry 2001, 40:1037-1043.
    • (2001) Biochemistry , vol.40 , pp. 1037-1043
    • Grimaldi, S.1    MacMillan, F.2    Ostermann, T.3    Ludwig, B.4    Michel, H.5    Prisner, T.6
  • 46
    • 0025264933 scopus 로고
    • Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli
    • Salerno J.C., Bolgiano B., Poole R.K., Gennis R.B., Ingledew W.J. Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli. J. Biol. Chem. 1990, 265:4364-4368.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4364-4368
    • Salerno, J.C.1    Bolgiano, B.2    Poole, R.K.3    Gennis, R.B.4    Ingledew, W.J.5
  • 48
    • 0001357106 scopus 로고    scopus 로고
    • 3 from Escherichia coli: kinetics of electron and proton transfer
    • 3 from Escherichia coli: kinetics of electron and proton transfer. Biochemistry 1997, 36:5425-5431.
    • (1997) Biochemistry , vol.36 , pp. 5425-5431
    • Ek, M.S.1    Brzezinski, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.