메뉴 건너뛰기




Volumn 3, Issue 2, 2009, Pages

Oxygen as acceptor

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84959079142     PISSN: None     EISSN: 23246200     Source Type: Journal    
DOI: 10.1128/ecosalplus.3.2.7     Document Type: Article
Times cited : (9)

References (244)
  • 1
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, ReznikoffWS, Riley M, Schaechter M, and Umbarger HE (ed), ASM Press, Washington, DC, 2nd ed
    • Gennis RB, Stewart V. 1996. Respiration, p 217-261. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, ReznikoffWS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 217-261
    • Gennis, R.B.1    Stewart, V.2
  • 2
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors
    • Unden G, Bongaerts J. 1997. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta 1320:217-234.
    • (1997) Biochim Biophys Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 5
    • 0034015380 scopus 로고    scopus 로고
    • Bacterial respiration: a flexible process for a changing environment
    • Richardson DJ. 2000. Bacterial respiration: a flexible process for a changing environment. Microbiology 146:551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 6
    • 65949120626 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase complex in Azotobacter vinelandii
    • (In Russian.)
    • Bertsova YV, Demin OV, Bogachev AV. 2005. Respiratory protection of nitrogenase complex in Azotobacter vinelandii. Usp Biol Khim 45:205-234. (In Russian.).
    • (2005) Usp Biol Khim , vol.45 , pp. 205-234
    • Bertsova, Y.V.1    Demin, O.V.2    Bogachev, A.V.3
  • 7
    • 0033928977 scopus 로고    scopus 로고
    • Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation
    • Poole RK, Cook GM. 2000. Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation. Adv Microb Physiol 43:165-224.
    • (2000) Adv Microb Physiol , vol.43 , pp. 165-224
    • Poole, R.K.1    Cook, G.M.2
  • 8
    • 0001383847 scopus 로고
    • The aerobic respiratory chain of Escherichia coli
    • Anraku Y, Gennis RB. 1987. The aerobic respiratory chain of Escherichia coli. Trends Biochem Sci 12:262-266.
    • (1987) Trends Biochem Sci , vol.12 , pp. 262-266
    • Anraku, Y.1    Gennis, R.B.2
  • 9
    • 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. 1998. Two terminal quinol oxidase families in Escherichia coli: variations on molecular machinery for dioxygen reduction. J Biochem Mol Biol Biophys 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
  • 10
    • 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
    • Cotter PA, Chepuri V, Gennis RB, Gunsalus RP. 1990. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol 172:6333-6338.
    • (1990) J Bacteriol , vol.172 , pp. 6333-6338
    • Cotter, P.A.1    Chepuri, V.2    Gennis, R.B.3    Gunsalus, R.P.4
  • 11
    • 0025754390 scopus 로고
    • The requirement of ArcA and Fnr for peak expression of the cyd operon in Escherichia coli under microaerobic conditions
    • Fu H-A, Iuchi S, Lin ECC. 1991. The requirement of ArcA and Fnr for peak expression of the cyd operon in Escherichia coli under microaerobic conditions. Mol Gen Genet 226:209-213.
    • (1991) Mol Gen Genet , vol.226 , pp. 209-213
    • Fu, H.-A.1    Iuchi, S.2    Lin, E.C.C.3
  • 12
    • 0017858515 scopus 로고
    • Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli
    • Rice CW, Hempfling WP. 1978. Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J Bacteriol 134:115-124.
    • (1978) J Bacteriol , vol.134 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 13
    • 33947369531 scopus 로고    scopus 로고
    • Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center
    • Yang K, Zhang J, Vakkasoglu AS, Hielscher R, Osborne JP, Hemp J, Miyoshi H, Hellwig P, Gennis RB. 2007. Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center. Biochemistry 46:3270-3278.
    • (2007) Biochemistry , vol.46 , pp. 3270-3278
    • Yang, K.1    Zhang, J.2    Vakkasoglu, A.S.3    Hielscher, R.4    Osborne, J.P.5    Hemp, J.6    Miyoshi, H.7    Hellwig, P.8    Gennis, R.B.9
  • 14
    • 0037046156 scopus 로고    scopus 로고
    • FTIR spectroscopic evidence for the involvement of an acidic residue in quinone binding in cytochrome bd from Escherichia coli
    • Zhang J, Oettmeier W, Gennis RB, Hellwig P. 2002. FTIR spectroscopic evidence for the involvement of an acidic residue in quinone binding in cytochrome bd from Escherichia coli. Biochemistry 41:4612-4617.
    • (2002) Biochemistry , vol.41 , pp. 4612-4617
    • Zhang, J.1    Oettmeier, W.2    Gennis, R.B.3    Hellwig, P.4
  • 16
    • 24044519364 scopus 로고    scopus 로고
    • Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability
    • Belevich I, Borisov VB, Konstantinov AA, Verkhovsky MI. 2005. Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability. FEBS Lett 579:4567-4570.
    • (2005) FEBS Lett , vol.579 , pp. 4567-4570
    • Belevich, I.1    Borisov, V.B.2    Konstantinov, A.A.3    Verkhovsky, M.I.4
  • 17
    • 0001357106 scopus 로고    scopus 로고
    • Oxidation of ubiquinol by cytochrome bo3 from Escherichia coli: kinetics of electron and proton transfer
    • Svensson-Ek M, Brzezinski P. 1997. Oxidation of ubiquinol by cytochrome bo3 from Escherichia coli: kinetics of electron and proton transfer. Biochemistry 36:5425-5431.
    • (1997) Biochemistry , vol.36 , pp. 5425-5431
    • Svensson-Ek, M.1    Brzezinski, P.2
  • 18
    • 0029981912 scopus 로고    scopus 로고
    • 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
    • D'mello R, Hill S, Poole RK. 1996. 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 142:755-763.
    • (1996) Microbiology , vol.142 , pp. 755-763
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 19
    • 0028909392 scopus 로고
    • The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin: Km values for oxygen are in the submicromolar range
    • D'mello R, Hill S, Poole RK. 1995. The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin: Km values for oxygen are in the submicromolar range. J Bacteriol 177:867-870.
    • (1995) J Bacteriol , vol.177 , pp. 867-870
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 20
    • 0028818107 scopus 로고
    • A suggested mechanism for the catalytic cycle of cytochrome bd ter-minal oxidase based on kinetic analysis
    • Junemann S, Butterworth PJ, Wrigglesworth JM. 1995. A suggested mechanism for the catalytic cycle of cytochrome bd ter-minal oxidase based on kinetic analysis. Biochemistry 34:14861-14867.
    • (1995) Biochemistry , vol.34 , pp. 14861-14867
    • Junemann, S.1    Butterworth, P.J.2    Wrigglesworth, J.M.3
  • 21
    • 0021272743 scopus 로고
    • Terminal oxidases of Escherichia coli aerobic respiratory chain. II. Purification and properties of cytochrome b558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems
    • Kita K, Konishi K, Anraku Y. 1984. Terminal oxidases of Escherichia coli aerobic respiratory chain. II. Purification and properties of cytochrome b558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems. J Biol Chem 259:3375-3381.
    • (1984) J Biol Chem , vol.259 , pp. 3375-3381
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 22
    • 0028332212 scopus 로고
    • Purification and characterization of the cytochrome bd complex from Azotobacter vinelandii: comparison to the complex from Escherichia coli
    • Kolonay JF Jr, Moshiri F, Gennis RB, Kaysser TM, Maier RJ. 1994. Purification and characterization of the cytochrome bd complex from Azotobacter vinelandii: comparison to the complex from Escherichia coli. J Bacteriol 176:4177-4181.
    • (1994) J Bacteriol , vol.176 , pp. 4177-4181
    • Kolonay, J.F.1    Moshiri, F.2    Gennis, R.B.3    Kaysser, T.M.4    Maier, R.J.5
  • 24
    • 0021280149 scopus 로고
    • Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth
    • Kita K, Konishi K, Anraku Y. 1984. Terminal oxidases of Escherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b562-o complex from cells in the early exponential phase of aerobic growth. J Biol Chem 259:3368-3374.
    • (1984) J Biol Chem , vol.259 , pp. 3368-3374
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 25
    • 0026129552 scopus 로고
    • E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli
    • Calhoun MW, Newton G, Gennis RB. 1991. E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli. J Bacteriol 173:1569-1570.
    • (1991) J Bacteriol , vol.173 , pp. 1569-1570
    • Calhoun, M.W.1    Newton, G.2    Gennis, R.B.3
  • 26
    • 0023802457 scopus 로고
    • The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli
    • Green GN, Fang H, Lin R-J, Newton G, Mather M, Georgiou CD, Gennis RB. 1988. The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli. J Biol Chem 263:13138-13143.
    • (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
  • 27
    • 0021039982 scopus 로고
    • Immunological characterization of an Escherichia coli strain which is lacking cytochrome d
    • Kranz RG, Barassi CA, Miller MJ, Green GN, Gennis RB. 1983. Immunological characterization of an Escherichia coli strain which is lacking cytochrome d. J Bacteriol 156:115-121.
    • (1983) J Bacteriol , vol.156 , pp. 115-121
    • Kranz, R.G.1    Barassi, C.A.2    Miller, M.J.3    Green, G.N.4    Gennis, R.B.5
  • 28
    • 0023196745 scopus 로고
    • Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli
    • Au DC-T, Gennis RB. 1987. Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli. J Bacteriol 169:3237-3242.
    • (1987) J Bacteriol , vol.169 , pp. 3237-3242
    • Au, D.C.-T.1    Gennis, R.B.2
  • 29
    • 0025293024 scopus 로고
    • The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of the cytochrome c oxidases
    • Chepuri V, Lemieux LJ, Au DC-T, Gennis RB. 1990. The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of the cytochrome c oxidases. J Biol Chem 265:11185-11192.
    • (1990) J Biol Chem , vol.265 , pp. 11185-11192
    • Chepuri, V.1    Lemieux, L.J.2    Au, D.C.-T.3    Gennis, R.B.4
  • 30
    • 0021099774 scopus 로고
    • The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain
    • Miller MJ, Gennis RB. 1983. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem 258:9159-9165.
    • (1983) J Biol Chem , vol.258 , pp. 9159-9165
    • Miller, M.J.1    Gennis, R.B.2
  • 31
    • 0026700972 scopus 로고
    • Modified, large-scale purification of the cytochrome o complex of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity
    • Minghetti KC, Goswitz VC, Gabriel NE, Hill JJ, Barassi C, Georgiou CD, Chan SI, Gennis RB. 1992. Modified, large-scale purification of the cytochrome o complex of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity. Biochemistry 31:6917-6924.
    • (1992) Biochemistry , vol.31 , pp. 6917-6924
    • Minghetti, K.C.1    Goswitz, V.C.2    Gabriel, N.E.3    Hill, J.J.4    Barassi, C.5    Georgiou, C.D.6    Chan, S.I.7    Gennis, R.B.8
  • 33
    • 0025264933 scopus 로고
    • Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli
    • Salerno JC, Bolgiano B, Poole RK, Gennis RB, Ingledew WJ. 1990. Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli. J Biol Chem 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
  • 34
    • 35349019174 scopus 로고    scopus 로고
    • Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement
    • Belevich I, Borisov VB, Verkhovsky MI. 2007. Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement. J Biol Chem 282:28514-28519.
    • (2007) J Biol Chem , vol.282 , pp. 28514-28519
    • Belevich, I.1    Borisov, V.B.2    Verkhovsky, M.I.3
  • 35
    • 14844351539 scopus 로고    scopus 로고
    • Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electronproton coupling in the di-heme active site
    • Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI. 2005. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electronproton coupling in the di-heme active site. Proc Natl Acad Sci USA 102:3657-3662.
    • (2005) Proc Natl Acad Sci USA , 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
  • 37
    • 0022383731 scopus 로고
    • The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli
    • Miller MJ, Gennis RB. 1985. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J Biol Chem 260:14003-14008.
    • (1985) J Biol Chem , vol.260 , pp. 14003-14008
    • Miller, M.J.1    Gennis, R.B.2
  • 38
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader M, Muse W, Ballou DP, Gassner C, Bardwell JCA. 1999. Oxidative protein folding is driven by the electron transport system. Cell 98:217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.A.5
  • 39
    • 0025347063 scopus 로고
    • Roles for enteric dtype cytochrome oxidase in N2 fixation and microaerobiosis
    • Hill S, Viollet S, Smith AT, Anthony C. 1990. Roles for enteric dtype cytochrome oxidase in N2 fixation and microaerobiosis. J Bacteriol 172:2071-2078.
    • (1990) J Bacteriol , vol.172 , pp. 2071-2078
    • Hill, S.1    Viollet, S.2    Smith, A.T.3    Anthony, C.4
  • 42
    • 0027391503 scopus 로고
    • Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase
    • Delaney JM, Wall D, Georgopoulos C. 1993. Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase. J Bacteriol 175:166-175.
    • (1993) J Bacteriol , vol.175 , pp. 166-175
    • Delaney, J.M.1    Wall, D.2    Georgopoulos, C.3
  • 43
    • 0026646181 scopus 로고
    • arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon
    • Wall D, Delaney JM, Fayet O, Lipinska B, Yamamoto T, Georgopoulos C. 1992. arc-dependent thermal regulation and extragenic suppression of the Escherichia coli cytochrome d operon. J Bacteriol 174:6554-6562.
    • (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
    • 0027439091 scopus 로고
    • Cytochrome d induction in Escherichia coli growing under unfavorable conditions
    • Bogachev AV, Murtazina RA, Skulachev VP. 1993. Cytochrome d induction in Escherichia coli growing under unfavorable conditions. FEBS Lett 336:75-78.
    • (1993) FEBS Lett , vol.336 , pp. 75-78
    • Bogachev, A.V.1    Murtazina, R.A.2    Skulachev, V.P.3
  • 46
    • 0016700183 scopus 로고
    • Synthesis of alternative membrane-bound redox carriers during aerobic growth of Escherichia coli in the presence of potassium cyanide
    • Ashcroft JR, Haddock BA. 1975. Synthesis of alternative membrane-bound redox carriers during aerobic growth of Escherichia coli in the presence of potassium cyanide. Biochem J 148:349-352.
    • (1975) Biochem J , vol.148 , pp. 349-352
    • Ashcroft, J.R.1    Haddock, B.A.2
  • 47
    • 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
    • Cook GM, Loder C, Soballe B, Stafford GP, Membrillo-Hernandez J, Poole RK. 1998. 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. Microbiology 144:3297-3308.
    • (1998) Microbiology , vol.144 , 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
  • 48
    • 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
    • Macinga DR, Rather PN. 1996. 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 19:511-520.
    • (1996) Mol Microbiol , vol.19 , pp. 511-520
    • Macinga, D.R.1    Rather, P.N.2
  • 49
    • 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
    • Siegele DA, Imlay KR, Imlay JA. 1996. The stationary-phase-exit defect of cydC (surB) mutants is due to the lack of a functional terminal cytochrome oxidase. J Bacteriol 178:6091-6096.
    • (1996) J Bacteriol , vol.178 , pp. 6091-6096
    • Siegele, D.A.1    Imlay, K.R.2    Imlay, J.A.3
  • 50
    • 0027715744 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant defective in resuming growth after starvation
    • Siegele DA, Kolter R. 1993. Isolation and characterization of an Escherichia coli mutant defective in resuming growth after starvation. Genes Dev 7:2629-2640.
    • (1993) Genes Dev , vol.7 , pp. 2629-2640
    • Siegele, D.A.1    Kolter, R.2
  • 52
    • 33747813904 scopus 로고    scopus 로고
    • Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase
    • Borisov VB, Forte E, Sarti P, Brunori M, Konstantinov AA, Giuffrè A. 2006. Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase. FEBS Lett 580:4823-4826.
    • (2006) FEBS Lett , vol.580 , pp. 4823-4826
    • Borisov, V.B.1    Forte, E.2    Sarti, P.3    Brunori, M.4    Konstantinov, A.A.5    Giuffrè, A.6
  • 54
    • 0028931296 scopus 로고
    • New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd
    • Meunier B, Madgwick SA, Reil E, Oettmeier W, Rich PR. 1995. New inhibitors of the quinol oxidation sites of bacterial cytochromes bo and bd. Biochemistry 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
  • 55
    • 44749089929 scopus 로고    scopus 로고
    • Gramicidin S identified as a potent inhibitor for cytochrome bd-type quinol oxidase
    • Mogi T, Ui H, Shiomi K, Omura S, Kita K. 2008. Gramicidin S identified as a potent inhibitor for cytochrome bd-type quinol oxidase. FEBS Lett 582:2299-2302.
    • (2008) FEBS Lett , vol.582 , pp. 2299-2302
    • Mogi, T.1    Ui, H.2    Shiomi, K.3    Omura, S.4    Kita, K.5
  • 56
    • 0030131933 scopus 로고    scopus 로고
    • Cytochrome bd: structure and properties
    • (Translated from Biokhimiya 61:786-799, 1996.)
    • Borisov VB. 1996. Cytochrome bd: structure and properties. Biochemistry (Moscow) 61:565-574. (Translated from Biokhimiya 61:786-799, 1996.).
    • (1996) Biochemistry (Moscow) , vol.61 , pp. 565-574
    • Borisov, V.B.1
  • 57
    • 0024299826 scopus 로고
    • Relationships between membrane-bound cytochrome o from Vitreoscilla and that of Escherichia coli
    • Georgiou C, Cokic P, Carter K, Webster DA, Gennis RB. 1988. Relationships between membrane-bound cytochrome o from Vitreoscilla and that of Escherichia coli. Biochim Biophys Acta 933:179-183.
    • (1988) Biochim Biophys Acta , vol.933 , pp. 179-183
    • Georgiou, C.1    Cokic, P.2    Carter, K.3    Webster, D.A.4    Gennis, R.B.5
  • 58
    • 0020803223 scopus 로고
    • Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from E. coli
    • Matsushita K, Patel L, Gennis RB, Kaback HR. 1983. Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from E. coli. Proc Natl Acad Sci USA 80:4889-4893.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4889-4893
    • Matsushita, K.1    Patel, L.2    Gennis, R.B.3    Kaback, H.R.4
  • 59
    • 0021770858 scopus 로고
    • Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation
    • Matsushita K, Patel L, Kaback HR. 1984. Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation. Biochemistry 23:4703-4714.
    • (1984) Biochemistry , vol.23 , pp. 4703-4714
    • Matsushita, K.1    Patel, L.2    Kaback, H.R.3
  • 60
    • 0025365339 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 8
    • Bachmann BJ. 1990. Linkage map of Escherichia coli K-12, edition 8. Microbiol Rev 54:130-197.
    • (1990) Microbiol Rev , vol.54 , pp. 130-197
    • Bachmann, B.J.1
  • 61
    • 0030809565 scopus 로고    scopus 로고
    • Assignment and functional roles of the cyoABCDE gene products required for the Escherichia coli bo-type quinol oxidase
    • Nakamura H, Saiki K, Mogi T, Anraku Y. 1997. Assignment and functional roles of the cyoABCDE gene products required for the Escherichia coli bo-type quinol oxidase. J Biochem (Tokyo) 122:415-421.
    • (1997) J Biochem (Tokyo) , vol.122 , pp. 415-421
    • Nakamura, H.1    Saiki, K.2    Mogi, T.3    Anraku, Y.4
  • 62
    • 0025301782 scopus 로고
    • Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the E. coli cytochrome o complex is in subunit I
    • Nakamura H, Yamoto I, Anraku Y, Lemieux L, Gennis RB. 1990. Expression of cyoA and cyoB demonstrates that the CO-binding heme component of the E. coli cytochrome o complex is in subunit I. J Biol Chem 265:11193-11197.
    • (1990) J Biol Chem , vol.265 , pp. 11193-11197
    • Nakamura, H.1    Yamoto, I.2    Anraku, Y.3    Lemieux, L.4    Gennis, R.B.5
  • 63
    • 0025640889 scopus 로고
    • Structural features of cytochrome oxidase
    • Saraste M. 1990. Structural features of cytochrome oxidase. Q Rev Biophys 23:331-366.
    • (1990) Q Rev Biophys , vol.23 , pp. 331-366
    • Saraste, M.1
  • 64
    • 0025306403 scopus 로고
    • The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli
    • Chepuri V, Gennis RB. 1990. The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli. J Biol Chem 265:12978-12986.
    • (1990) J Biol Chem , vol.265 , pp. 12978-12986
    • Chepuri, V.1    Gennis, R.B.2
  • 65
    • 0030915266 scopus 로고    scopus 로고
    • Exploring subunit-subunit interactions in the Escherichia coli bo-type ubiquinol oxidase by extragenic suppressor mutation analysis
    • Saiki K, Mogi T, Tsubaki M, Hori H, Anraku Y. 1997. Exploring subunit-subunit interactions in the Escherichia coli bo-type ubiquinol oxidase by extragenic suppressor mutation analysis. J Biol Chem 272:14721-14726.
    • (1997) J Biol Chem , vol.272 , pp. 14721-14726
    • Saiki, K.1    Mogi, T.2    Tsubaki, M.3    Hori, H.4    Anraku, Y.5
  • 66
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana J, Lübben M, Saraste M, Higgins DG. 1994. Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J 13:2516-2525.
    • (1994) EMBO J , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lübben, M.2    Saraste, M.3    Higgins, D.G.4
  • 67
    • 0028152645 scopus 로고
    • Biosynthesis and functional role of haem O and haem A
    • Mogi T, Saiki K, Anraku Y. 1994. Biosynthesis and functional role of haem O and haem A. Mol Microbiol 14:391-398.
    • (1994) Mol Microbiol , vol.14 , pp. 391-398
    • Mogi, T.1    Saiki, K.2    Anraku, Y.3
  • 68
    • 0027086985 scopus 로고
    • Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase
    • Saiki K, Mogi T, Anraku Y. 1992. Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase. Biochem Biophys Res Commun 189:1491-1497.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1491-1497
    • Saiki, K.1    Mogi, T.2    Anraku, Y.3
  • 69
    • 0027442655 scopus 로고
    • In vitro heme O synthesis by the cyoE gene product from Escherichia coli
    • Saiki K, Mogi T, Ogura K, Anraku Y. 1993. In vitro heme O synthesis by the cyoE gene product from Escherichia coli. J Biol Chem 268:26041-26045.
    • (1993) J Biol Chem , vol.268 , pp. 26041-26045
    • Saiki, K.1    Mogi, T.2    Ogura, K.3    Anraku, Y.4
  • 70
    • 0026542614 scopus 로고
    • Determination of the ligands of the low-spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis
    • Lemieux LJ, Calhoun MW, Thomas JW, Ingledew WJ, Gennis RB. 1992. Determination of the ligands of the low-spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis. J Biol Chem 267:2105-2113.
    • (1992) J Biol Chem , vol.267 , pp. 2105-2113
    • Lemieux, L.J.1    Calhoun, M.W.2    Thomas, J.W.3    Ingledew, W.J.4    Gennis, R.B.5
  • 71
    • 0026507536 scopus 로고
    • Identification of heme ligands in subunit I of the cytochrome bo complex in Escherichia coli
    • Minagawa J, Mogi T, Gennis RB, Anraku Y. 1992. Identification of heme ligands in subunit I of the cytochrome bo complex in Escherichia coli. J Biol Chem 267:2096-2104.
    • (1992) J Biol Chem , vol.267 , pp. 2096-2104
    • Minagawa, J.1    Mogi, T.2    Gennis, R.B.3    Anraku, Y.4
  • 72
    • 0029999853 scopus 로고    scopus 로고
    • Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses
    • Saiki K, Nakamura H, Mogi T, Anraku Y. 1996. Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. J Biol Chem 271:15336-15340.
    • (1996) J Biol Chem , vol.271 , pp. 15336-15340
    • Saiki, K.1    Nakamura, H.2    Mogi, T.3    Anraku, Y.4
  • 73
    • 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
    • Miller MJ, Hermodson M, Gennis RB. 1988. 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 263:5235-5240.
    • (1988) J Biol Chem , vol.263 , pp. 5235-5240
    • Miller, M.J.1    Hermodson, M.2    Gennis, R.B.3
  • 74
    • 0021690885 scopus 로고
    • Cloning the cyd gene locus coding for the cytochrome d complex of Escherichia coli
    • Green GN, Kranz JE, Gennis RB. 1984. Cloning the cyd gene locus coding for the cytochrome d complex of Escherichia coli. Gene 32:99-106.
    • (1984) Gene , vol.32 , pp. 99-106
    • Green, G.N.1    Kranz, J.E.2    Gennis, R.B.3
  • 75
    • 0028048861 scopus 로고
    • Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation
    • Poole RK. 1994. Oxygen reactions with bacterial oxidases and globins: binding, reduction and regulation. Antonie van Leeuwenhoek 65:289-310.
    • (1994) Antonie van Leeuwenhoek , vol.65 , pp. 289-310
    • Poole, R.K.1
  • 76
    • 0022470314 scopus 로고
    • Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595
    • Lorence RM, Koland JG, Gennis RB. 1986. Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595. Biochemistry 25:2314-2321.
    • (1986) Biochemistry , vol.25 , pp. 2314-2321
    • Lorence, R.M.1    Koland, J.G.2    Gennis, R.B.3
  • 77
    • 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
    • Newton G, Gennis RB. 1991. 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 1089:8-12.
    • (1991) Biochim Biophys Acta , vol.1089 , pp. 8-12
    • Newton, G.1    Gennis, R.B.2
  • 78
    • 0022542231 scopus 로고
    • The specific overproduction and purification of the cytochrome b558 component of the cytochrome d complex from Escherichia coli
    • Green GN, Lorence RM, Gennis RB. 1986. The specific overproduction and purification of the cytochrome b558 component of the cytochrome d complex from Escherichia coli. Biochemistry 25:2309-2314.
    • (1986) Biochemistry , vol.25 , pp. 2309-2314
    • Green, G.N.1    Lorence, R.M.2    Gennis, R.B.3
  • 79
    • 0023276114 scopus 로고
    • Identification of the cydC locus required for the expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli
    • Georgiou CD, Fang H, Gennis RB. 1987. 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 169:2107-2112.
    • (1987) J Bacteriol , vol.169 , pp. 2107-2112
    • Georgiou, C.D.1    Fang, H.2    Gennis, R.B.3
  • 80
    • 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
    • Poole RK, Hatch L, Cleeter MWJ, Gibson F, Cox GB, Wu G. 1993. 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 10:421-430.
    • (1993) Mol Microbiol , vol.10 , 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
  • 81
    • 17944386101 scopus 로고
    • Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: identification and mapping of a fourth locus, cydD
    • Poole RK, Williams HD, Downie JA, Gibson F. 1989. Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: identification and mapping of a fourth locus, cydD. J Gen Microbiol 135:1865-1874.
    • (1989) J Gen Microbiol , vol.135 , pp. 1865-1874
    • Poole, R.K.1    Williams, H.D.2    Downie, J.A.3    Gibson, F.4
  • 82
    • 0027303826 scopus 로고
    • Investigation of the role of the cydD gene product in production of a functional cytochrome d oxidase in Escherichia coli
    • Bebbington KJ, Williams HD. 1993. Investigation of the role of the cydD gene product in production of a functional cytochrome d oxidase in Escherichia coli. FEMS Microbiol Lett 112:19-24.
    • (1993) FEMS Microbiol Lett , vol.112 , pp. 19-24
    • Bebbington, K.J.1    Williams, H.D.2
  • 83
    • 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
    • Poole RK, Gibson F, Wu G. 1994. 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 117:217-224.
    • (1994) FEMS Microbiol Lett , vol.117 , pp. 217-224
    • Poole, R.K.1    Gibson, F.2    Wu, G.3
  • 84
    • 25444517605 scopus 로고    scopus 로고
    • A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm
    • Pittman MS, Robinson HC, Poole RK. 2005. A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm. J Biol Chem 280:32254-32261.
    • (2005) J Biol Chem , vol.280 , pp. 32254-32261
    • Pittman, M.S.1    Robinson, H.C.2    Poole, R.K.3
  • 85
    • 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 PA, Gunsalus RP. 1992. 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 91:31-36.
    • (1992) FEMS Microbiol Lett , vol.91 , pp. 31-36
    • Cotter, P.A.1    Gunsalus, R.P.2
  • 86
    • 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
    • Cotter PA, Melville SB, Albrecht JA, Gunsalus RP. 1997. Aerobic regulation of cytochrome d oxidase (cydAB) operon expression in Escherichia coli: roles of Fnr and ArcA in repression and activation. Mol Microbiol 25:605-615.
    • (1997) Mol Microbiol , vol.25 , pp. 605-615
    • Cotter, P.A.1    Melville, S.B.2    Albrecht, J.A.3    Gunsalus, R.P.4
  • 87
    • 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
    • Govantes F, Albrecht JA, Gunsalus RP. 2000. 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 37:1456-1469.
    • (2000) Mol Microbiol , vol.37 , pp. 1456-1469
    • Govantes, F.1    Albrecht, J.A.2    Gunsalus, R.P.3
  • 88
    • 0026539733 scopus 로고
    • Control of electron flow in Escherichia coli: coordinated transcription of respiratory pathway genes
    • Gunsalus RP. 1992. Control of electron flow in Escherichia coli: coordinated transcription of respiratory pathway genes. J Bacteriol 174:7069-7074.
    • (1992) J Bacteriol , vol.174 , pp. 7069-7074
    • Gunsalus, R.P.1
  • 89
    • 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
    • Iuchi S, Chepuri V, Fu H-A, Gennis RB, Lin ECC. 1990. 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 172:6020-6025.
    • (1990) J Bacteriol , vol.172 , pp. 6020-6025
    • Iuchi, S.1    Chepuri, V.2    Fu, H.-A.3    Gennis, R.B.4    Lin, E.C.C.5
  • 90
    • 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
    • Shalel-Levanon S, San KY, Bennett GN. 2005. 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 7:364-374.
    • (2005) Metab Eng , vol.7 , pp. 364-374
    • Shalel-Levanon, S.1    San, K.Y.2    Bennett, G.N.3
  • 91
    • 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 RP. 1996. 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 178:1094-1098.
    • (1996) J Bacteriol , vol.178 , pp. 1094-1098
    • Tseng, C.-P.1    Albrecht, J.2    Gunsalus, R.P.3
  • 92
    • 0001104525 scopus 로고    scopus 로고
    • Responses to molecular oxygen
    • Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, ReznikoffWS, Riley M, Schaechter M, and Umbarger HE (ed), ASM Press, Washington, DC, 2nd ed
    • Lynch AS, Lin ECC. 1996. Responses to molecular oxygen, p 1526-1538. In Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, ReznikoffWS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1526-1538
    • Lynch, A.S.1    Lin, E.C.C.2
  • 93
    • 0035933597 scopus 로고    scopus 로고
    • Quinones as the redox signal for the arc two-component system of bacteria
    • Georgellis D, Kwon O, Lin EC. 2001. Quinones as the redox signal for the arc two-component system of bacteria. Science 292:2314-2316.
    • (2001) Science , vol.292 , pp. 2314-2316
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.3
  • 94
    • 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
    • Georgellis D, Kwon O, Lin EC. 1999. 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 274:35950-35954.
    • (1999) J Biol Chem , vol.274 , pp. 35950-35954
    • Georgellis, D.1    Kwon, O.2    Lin, E.C.3
  • 95
    • 0037216801 scopus 로고    scopus 로고
    • Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions
    • Alexeeva S, Hellingwerf KJ, Teixeira de Mattos MJ. 2003. Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions. J Bacteriol 185:204-209.
    • (2003) J Bacteriol , vol.185 , pp. 204-209
    • Alexeeva, S.1    Hellingwerf, K.J.2    Teixeira de Mattos, M.J.3
  • 96
    • 0032457906 scopus 로고    scopus 로고
    • Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster
    • Kiley PJ, Beinert H. 1998. Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster. FEMS Microbiol Rev 22:341-352.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 341-352
    • Kiley, P.J.1    Beinert, H.2
  • 97
    • 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
    • Overton TW, Griffiths L, Patel MD, Hobman JL, Penn CW, Cole JA, Constantinidou C. 2006. 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 34:104-107.
    • (2006) Biochem Soc Trans , vol.34 , 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
  • 98
    • 0029664739 scopus 로고    scopus 로고
    • O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli
    • Becker S, Holighaus G, Gabrielczyk T, Unden G. 1996. O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli. J Bacteriol 178:4515-4521.
    • (1996) J Bacteriol , vol.178 , pp. 4515-4521
    • Becker, S.1    Holighaus, G.2    Gabrielczyk, T.3    Unden, G.4
  • 99
    • 0019490792 scopus 로고
    • Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication
    • Collins MD, Jones D. 1981. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication. Microbiol Rev 45:316-354.
    • (1981) Microbiol Rev , vol.45 , pp. 316-354
    • Collins, M.D.1    Jones, D.2
  • 100
    • 0031041808 scopus 로고    scopus 로고
    • Aeration-dependent changes in composition of the quinone pool in Escherichia coli. Evidence of post-transcriptional regulation of the quinone biosynthesis
    • Shestopalov AI, Bogachev AV, Murtazina RA, Viryasov MB, Skulachev VP. 1997. Aeration-dependent changes in composition of the quinone pool in Escherichia coli. Evidence of post-transcriptional regulation of the quinone biosynthesis. FEBS Lett 404:272-274.
    • (1997) FEBS Lett , vol.404 , pp. 272-274
    • Shestopalov, A.I.1    Bogachev, A.V.2    Murtazina, R.A.3    Viryasov, M.B.4    Skulachev, V.P.5
  • 101
    • 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. 1994. Identification of a novel quinone binding site in the cytochrome bo complex from Escherichia coli. J Biol Chem 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
  • 102
    • 33845923707 scopus 로고    scopus 로고
    • Glutamates 99 and 107 in transmembrane helix III of subunit I of cytochrome bd are critical for binding of the heme b595-d binuclear center and enzyme activity
    • Mogi T, Endou S, Akimoto S, Morimoto-Tadokoro M, Miyoshi H. 2006. Glutamates 99 and 107 in transmembrane helix III of subunit I of cytochrome bd are critical for binding of the heme b595-d binuclear center and enzyme activity. Biochemistry 45:15785-15792.
    • (2006) Biochemistry , vol.45 , pp. 15785-15792
    • Mogi, T.1    Endou, S.2    Akimoto, S.3    Morimoto-Tadokoro, M.4    Miyoshi, H.5
  • 105
    • 0033517852 scopus 로고    scopus 로고
    • Vibrational modes of ubiquinone in cytochrome bo3 from Escherichia coli identified by Fourier transform infrared difference spectroscopy and specific 13C labeling
    • Hellwig P, Mogi T, Tomson FL, Gennis RB, Iwata J, Miyoshi H, Mäntele W. 1999. Vibrational modes of ubiquinone in cytochrome bo3 from Escherichia coli identified by Fourier transform infrared difference spectroscopy and specific 13C labeling. Biochemistry 38:14683-14689.
    • (1999) Biochemistry , vol.38 , pp. 14683-14689
    • Hellwig, P.1    Mogi, T.2    Tomson, F.L.3    Gennis, R.B.4    Iwata, J.5    Miyoshi, H.6    Mäntele, W.7
  • 106
    • 0037183474 scopus 로고    scopus 로고
    • Identification of the residues involved in stabilization of the semiquinone radical in the high-affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli by site-directed mutagenesis and EPR spectroscopy
    • Hellwig P, Yano T, Ohnishi T, Gennis RB. 2002. Identification of the residues involved in stabilization of the semiquinone radical in the high-affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli by site-directed mutagenesis and EPR spectroscopy. Biochemistry 41:10675-10679.
    • (2002) Biochemistry , vol.41 , pp. 10675-10679
    • Hellwig, P.1    Yano, T.2    Ohnishi, T.3    Gennis, R.B.4
  • 108
    • 0019883170 scopus 로고
    • Coordination geometries and vibrational properties of cytochromes a and a3 in cytochrome oxidase from Soret excitation Raman spectroscopy
    • Babcock GT, Callahan PM, Ondrias MR, Salmeen I. 1981. Coordination geometries and vibrational properties of cytochromes a and a3 in cytochrome oxidase from Soret excitation Raman spectroscopy. Biochemistry 20:959-966.
    • (1981) Biochemistry , vol.20 , pp. 959-966
    • Babcock, G.T.1    Callahan, P.M.2    Ondrias, M.R.3    Salmeen, I.4
  • 109
    • 0024601949 scopus 로고
    • Potentiometric titration of cytochrome-bo type quinol oxidase of Escherichia coli: evidence for heme-heme and copper-heme interaction
    • Salerno JC, Bolgiano B, Ingledew WJ. 1989. Potentiometric titration of cytochrome-bo type quinol oxidase of Escherichia coli: evidence for heme-heme and copper-heme interaction. FEBS Lett 247:101-105.
    • (1989) FEBS Lett , vol.247 , pp. 101-105
    • Salerno, J.C.1    Bolgiano, B.2    Ingledew, W.J.3
  • 111
    • 0017049582 scopus 로고
    • Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives
    • Babcock GT, Vickery LE, Palmer G. 1976. Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives. J Biol Chem 251:7907-7919.
    • (1976) J Biol Chem , vol.251 , pp. 7907-7919
    • Babcock, G.T.1    Vickery, L.E.2    Palmer, G.3
  • 113
    • 0033528667 scopus 로고    scopus 로고
    • Cu XAS shows a change in the ligation of CuB upon reduction of cytochrome bo3 from Escherichia coli
    • Osborne JP, Cosper NJ, Stalhandske CM, Scott RA, Alben JO, Gennis RB. 1999. Cu XAS shows a change in the ligation of CuB upon reduction of cytochrome bo3 from Escherichia coli. Biochemistry 38:4526-4532.
    • (1999) Biochemistry , vol.38 , pp. 4526-4532
    • Osborne, J.P.1    Cosper, N.J.2    Stalhandske, C.M.3    Scott, R.A.4    Alben, J.O.5    Gennis, R.B.6
  • 114
    • 0033137318 scopus 로고    scopus 로고
    • Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor?
    • Ralle M, Verkhovskaya ML, Morgan JE, Verkhovsky MI, Wikström M, Blackburn NJ. 1999. Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor? Biochemistry 38:7185-7194.
    • (1999) Biochemistry , vol.38 , pp. 7185-7194
    • Ralle, M.1    Verkhovskaya, M.L.2    Morgan, J.E.3    Verkhovsky, M.I.4    Wikström, M.5    Blackburn, N.J.6
  • 115
    • 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. 1994. 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 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
  • 116
    • 0028877684 scopus 로고
    • Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo
    • Ingledew WJ, Ohnishi T, Salerno JC. 1995. Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo. Eur J Biochem 227:903-908.
    • (1995) Eur J Biochem , vol.227 , pp. 903-908
    • Ingledew, W.J.1    Ohnishi, T.2    Salerno, J.C.3
  • 117
    • 0028788464 scopus 로고
    • Stabiization of a semiquinone radical at the highaffinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase
    • Sato-Watanabe M, Itoh S, Mogi T, Matsuura K, Miyoshi H, Anraku Y. 1995. Stabiization of a semiquinone radical at the highaffinity quinone-binding site (QH) of the Escherichia coli bo-type ubiquinol oxidase. FEBS Lett 374:265-269.
    • (1995) FEBS Lett , vol.374 , pp. 265-269
    • Sato-Watanabe, M.1    Itoh, S.2    Mogi, T.3    Matsuura, K.4    Miyoshi, H.5    Anraku, Y.6
  • 118
    • 0028625501 scopus 로고
    • The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli
    • Hill BC, Hill JJ, Gennis RB. 1994. The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli. Biochemistry 33:15110-15115.
    • (1994) Biochemistry , vol.33 , pp. 15110-15115
    • Hill, B.C.1    Hill, J.J.2    Gennis, R.B.3
  • 119
    • 0026337648 scopus 로고
    • Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectrosopy
    • Kahlow MA, Zuberi TM, Gennis RB, Loehr TM. 1991. Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectrosopy. Biochemistry 30:11485-11489.
    • (1991) Biochemistry , vol.30 , pp. 11485-11489
    • Kahlow, M.A.1    Zuberi, T.M.2    Gennis, R.B.3    Loehr, T.M.4
  • 120
    • 0024976978 scopus 로고
    • EPR studies of the cytochrome-d complex of Escherichia coli
    • Meinhardt SW, Gennis RB, Ohnishi T. 1989. EPR studies of the cytochrome-d complex of Escherichia coli. Biochim Biophys Acta 975:175-184.
    • (1989) Biochim Biophys Acta , vol.975 , pp. 175-184
    • Meinhardt, S.W.1    Gennis, R.B.2    Ohnishi, T.3
  • 121
    • 0024348253 scopus 로고
    • The cytochromes of anaerobically grown Escherichia coli
    • Rothery R, Ingledew WJ. 1989. The cytochromes of anaerobically grown Escherichia coli. Biochem J 262:437-443.
    • (1989) Biochem J , vol.262 , pp. 437-443
    • Rothery, R.1    Ingledew, W.J.2
  • 122
    • 17144445848 scopus 로고
    • The respiratory chain of anaerobically grown Escherichia coli: reactions with nitrite and oxygen
    • Rothery RA, Houston AM, Ingledew WJ. 1987. The respiratory chain of anaerobically grown Escherichia coli: reactions with nitrite and oxygen. J Gen Microbiol 133:3247-3255.
    • (1987) J Gen Microbiol , vol.133 , pp. 3247-3255
    • Rothery, R.A.1    Houston, A.M.2    Ingledew, W.J.3
  • 123
    • 0026580478 scopus 로고
    • The orientation of the three haems of the in situ ubiquinol oxidase, cytochrome bd, of Escherichia coli
    • Ingledew WJ, Rothery RA, Gennis RB, Salerno JC. 1992. The orientation of the three haems of the in situ ubiquinol oxidase, cytochrome bd, of Escherichia coli. Biochem J 282:255-259.
    • (1992) Biochem J , vol.282 , pp. 255-259
    • Ingledew, W.J.1    Rothery, R.A.2    Gennis, R.B.3    Salerno, J.C.4
  • 124
    • 0025259440 scopus 로고
    • Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize a functional domain
    • Dueweke TJ, Gennis RB. 1990. Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize a functional domain. J Biol Chem 265:4273-4277.
    • (1990) J Biol Chem , vol.265 , pp. 4273-4277
    • Dueweke, T.J.1    Gennis, R.B.2
  • 125
    • 0021251072 scopus 로고
    • Characterization of the cytochrome d terminal oxidase complex of Escherichia coli using polyclonal and monoclonal antibodies
    • Kranz RG, Gennis RB. 1984. Characterization of the cytochrome d terminal oxidase complex of Escherichia coli using polyclonal and monoclonal antibodies. J Biol Chem 259:7998-8003.
    • (1984) J Biol Chem , vol.259 , pp. 7998-8003
    • Kranz, R.G.1    Gennis, R.B.2
  • 126
    • 0025881879 scopus 로고
    • Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localizes a quinol oxidase domain
    • Dueweke TJ, Gennis RB. 1991. Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localizes a quinol oxidase domain. Biochemistry 30:3401-3406.
    • (1991) Biochemistry , vol.30 , pp. 3401-3406
    • Dueweke, T.J.1    Gennis, R.B.2
  • 127
    • 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
    • Lorence RM, Carter K, Gennis RB, Matsushita K, Kaback HR. 1988. 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 11:5271-5276.
    • (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
  • 128
    • 0003120348 scopus 로고
    • Bacterial cytochrome oxidases
    • Anthony C (ed), Academic Press, London, United Kingdom
    • Poole RK. 1988. Bacterial cytochrome oxidases, p 231-291. In Anthony C (ed), Bacterial Energy Transduction. Academic Press, London, United Kingdom.
    • (1988) Bacterial Energy Transduction , pp. 231-291
    • Poole, R.K.1
  • 129
    • 0000370757 scopus 로고
    • Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli
    • Koland JG, Miller MJ, Gennis RB. 1984. Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli. Biochemistry 23:1051-1056.
    • (1984) Biochemistry , vol.23 , pp. 1051-1056
    • Koland, J.G.1    Miller, M.J.2    Gennis, R.B.3
  • 130
    • 0033547815 scopus 로고    scopus 로고
    • Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands
    • Borisov V, Arutyunyan AM, Osborne JP, Gennis RB, Konstantinov AA. 1999. Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands. Biochemistry 38:740-750.
    • (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
  • 131
    • 0024411033 scopus 로고
    • Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis
    • Fang H, Lin R-J, Gennis RB. 1989. Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis. J Biol Chem 264:8026-8032.
    • (1989) J Biol Chem , vol.264 , pp. 8026-8032
    • Fang, H.1    Lin, R.-J.2    Gennis, R.B.3
  • 132
    • 0028863973 scopus 로고
    • Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli
    • Kaysser TM, Ghaim JB, Georgiou C, Gennis RB. 1995. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli. Biochemistry 34:13491-13501.
    • (1995) Biochemistry , vol.34 , pp. 13491-13501
    • Kaysser, T.M.1    Ghaim, J.B.2    Georgiou, C.3    Gennis, R.B.4
  • 133
    • 0028989001 scopus 로고
    • The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation
    • Spinner F, Cheesman MR, Thomson AJ, Kaysser T, Gennis RB, Peng Q, Peterson J. 1995. The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation. Biochem J 308:641-644.
    • (1995) Biochem J , vol.308 , pp. 641-644
    • Spinner, F.1    Cheesman, M.R.2    Thomson, A.J.3    Kaysser, T.4    Gennis, R.B.5    Peng, Q.6    Peterson, J.7
  • 134
    • 0033044722 scopus 로고    scopus 로고
    • Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunits I
    • Osborne JP, Gennis RB. 1999. Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunits I. Biochim Biophys Acta 1410:32-50.
    • (1999) Biochim Biophys Acta , vol.1410 , pp. 32-50
    • Osborne, J.P.1    Gennis, R.B.2
  • 135
    • 1542346467 scopus 로고    scopus 로고
    • Gene fusions with β-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface
    • Zhang J, Barquera B, Gennis RB. 2004. Gene fusions with β-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface. FEBS Lett 561:58-62.
    • (2004) FEBS Lett , vol.561 , pp. 58-62
    • Zhang, J.1    Barquera, B.2    Gennis, R.B.3
  • 136
    • 0021104863 scopus 로고
    • Bacterial cytochrome oxidases: a structurally and functionally diverse group of electron transfer proteins
    • Poole RK. 1983. Bacterial cytochrome oxidases: a structurally and functionally diverse group of electron transfer proteins. Biochim Biophys Acta 726:205-243.
    • (1983) Biochim Biophys Acta , vol.726 , pp. 205-243
    • Poole, R.K.1
  • 137
    • 0034652126 scopus 로고    scopus 로고
    • Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site?
    • Vos MH, Borisov VB, Liebl U, Martin J-L, Konstantinov AA. 2000. Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site? Proc Natl Acad Sci USA 97:1554-1559.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1554-1559
    • Vos, M.H.1    Borisov, V.B.2    Liebl, U.3    Martin, J.-L.4    Konstantinov, A.A.5
  • 138
    • 0030030899 scopus 로고    scopus 로고
    • Resonance Raman spectroscopic identification of a histidine ligand of b595 and the nature of the ligation of chlorin d in the fully reduced Escherichia coli cytochrome bd oxidase
    • Sun J, Kahlow MA, Kaysser TM, Osborne JP, Hill JJ, Rohlfs RJ, Hille R, Gennis RB, Loehr TM. 1996. Resonance Raman spectroscopic identification of a histidine ligand of b595 and the nature of the ligation of chlorin d in the fully reduced Escherichia coli cytochrome bd oxidase. Biochemistry 35:2403-2412.
    • (1996) Biochemistry , vol.35 , pp. 2403-2412
    • Sun, J.1    Kahlow, M.A.2    Kaysser, T.M.3    Osborne, J.P.4    Hill, J.J.5    Rohlfs, R.J.6    Hille, R.7    Gennis, R.B.8    Loehr, T.M.9
  • 139
    • 0007452186 scopus 로고
    • Interaction of cytochrome bd from Escherichia coli with hydrogen peroxide
    • (Translated from Biokhimiya 60:315-327, 1995.)
    • Borisov VB, Gennis RB, Konstantinov AA. 1995. Interaction of cytochrome bd from Escherichia coli with hydrogen peroxide. Biochemistry (Moscow) 60:231-239. (Translated from Biokhimiya 60:315-327, 1995.).
    • (1995) Biochemistry (Moscow) , vol.60 , pp. 231-239
    • Borisov, V.B.1    Gennis, R.B.2    Konstantinov, A.A.3
  • 140
    • 0037022192 scopus 로고    scopus 로고
    • Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy
    • Borisov VB, Liebl U, Rappaport F, Martin J-L, Zhang J, Gennis RB, Konstantinov AA, Vos MH. 2002. Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy. Biochemistry 41:1654-1662.
    • (2002) Biochemistry , vol.41 , pp. 1654-1662
    • Borisov, V.B.1    Liebl, U.2    Rappaport, F.3    Martin, J.-L.4    Zhang, J.5    Gennis, R.B.6    Konstantinov, A.A.7    Vos, M.H.8
  • 141
    • 0035933874 scopus 로고    scopus 로고
    • Interaction of cytochrome bd with carbon monoxide at low and room temperatures: evidence that only a small fraction of heme b595 reacts with CO
    • Borisov VB, Sedelnikova SE, Poole RK, Konstantinov AA. 2001. Interaction of cytochrome bd with carbon monoxide at low and room temperatures: evidence that only a small fraction of heme b595 reacts with CO. J Biol Chem 276:22095-22099.
    • (2001) J Biol Chem , vol.276 , pp. 22095-22099
    • Borisov, V.B.1    Sedelnikova, S.E.2    Poole, R.K.3    Konstantinov, A.A.4
  • 142
    • 0027299607 scopus 로고
    • Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
    • Hill JJ, Alben JO, Gennis RB. 1993. Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc Natl Acad Sci USA 90:5863-5867.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5863-5867
    • Hill, J.J.1    Alben, J.O.2    Gennis, R.B.3
  • 143
    • 0028791167 scopus 로고
    • Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli
    • Tsubaki M, Hori H, Mogi T, Anraku Y. 1995. Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli. J Biol Chem 270:28565-28569.
    • (1995) J Biol Chem , vol.270 , pp. 28565-28569
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3    Anraku, Y.4
  • 144
    • 38949194251 scopus 로고    scopus 로고
    • Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: the Fe-to-Fe distance between hemes d and b595 is 10 Å
    • Arutyunyan AM, Borisov VB, Novoderezhkin VI, Ghaim J, Zhang J, Gennis RB, Konstantinov AA. 2008. Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: the Fe-to-Fe distance between hemes d and b595 is 10 Å. Biochemistry 47:1752-1759.
    • (2008) Biochemistry , vol.47 , pp. 1752-1759
    • Arutyunyan, A.M.1    Borisov, V.B.2    Novoderezhkin, V.I.3    Ghaim, J.4    Zhang, J.5    Gennis, R.B.6    Konstantinov, A.A.7
  • 145
    • 0023650036 scopus 로고
    • Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli
    • Hata-Tanaka A, Matsuura K, Itoh S, Anraku Y. 1987. Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli. Biochim Biophys Acta 893:289-295.
    • (1987) Biochim Biophys Acta , vol.893 , pp. 289-295
    • Hata-Tanaka, A.1    Matsuura, K.2    Itoh, S.3    Anraku, Y.4
  • 146
    • 0023648080 scopus 로고
    • Proposal that the function of the membrane-bound cytochrome a1-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d
    • Poole RK, Williams HD. 1987. Proposal that the function of the membrane-bound cytochrome a1-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d. FEBS Lett 217:49-52.
    • (1987) FEBS Lett , vol.217 , pp. 49-52
    • Poole, R.K.1    Williams, H.D.2
  • 147
    • 33845378891 scopus 로고
    • Proposed structure of heme d, a prosthetic group of bacterial terminal oxidases
    • Timkovich R, Cork MS, Gennis RB, Johnson PY. 1985. Proposed structure of heme d, a prosthetic group of bacterial terminal oxidases. J Am Chem Soc 107:6069-6075.
    • (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
  • 148
    • 84984233402 scopus 로고
    • Resonance Raman study on axial ligands of heme irons in cytochrome bd-type ubiquinol oxidase from Escherichia coli
    • Hirota S, Mogi T, Anraku Y, Gennis RB, Kitagawa T. 1995. Resonance Raman study on axial ligands of heme irons in cytochrome bd-type ubiquinol oxidase from Escherichia coli. Biospectroscopy 1:305-311.
    • (1995) Biospectroscopy , vol.1 , pp. 305-311
    • Hirota, S.1    Mogi, T.2    Anraku, Y.3    Gennis, R.B.4    Kitagawa, T.5
  • 150
    • 0029942493 scopus 로고    scopus 로고
    • EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli
    • Hori H, Tsubaki M, Mogi T, Anraku Y. 1996. EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli. J Biol Chem 271:9254-9258.
    • (1996) J Biol Chem , vol.271 , pp. 9254-9258
    • Hori, H.1    Tsubaki, M.2    Mogi, T.3    Anraku, Y.4
  • 151
    • 48249119551 scopus 로고    scopus 로고
    • Glutamate 107 in subunit I of cytochrome bd from Escherichia coli is part of a transmembrane intraprotein pathway conducting protons from the cytoplasm to the heme b595/heme d active site
    • Borisov VB, Belevich I, Bloch DA, Mogi T, Verkhovsky MI. 2008. Glutamate 107 in subunit I of cytochrome bd from Escherichia coli is part of a transmembrane intraprotein pathway conducting protons from the cytoplasm to the heme b595/heme d active site. Biochemistry 47:7907-7914.
    • (2008) Biochemistry , vol.47 , pp. 7907-7914
    • Borisov, V.B.1    Belevich, I.2    Bloch, D.A.3    Mogi, T.4    Verkhovsky, M.I.5
  • 152
    • 0017175074 scopus 로고
    • Redox potentials of the cytochromes in the respiratory chain of aerobically grown Escherichia coli
    • Pudek MR, Bragg PD. 1976. Redox potentials of the cytochromes in the respiratory chain of aerobically grown Escherichia coli. Arch Biochem Biophys 174:546-552.
    • (1976) Arch Biochem Biophys , vol.174 , pp. 546-552
    • Pudek, M.R.1    Bragg, P.D.2
  • 153
    • 0021769529 scopus 로고
    • Effects of pH and detergent on the kinetic and electrochemical properties of the purified cytochrome d complex of Escherichia coli
    • Lorence RM, Miller MJ, Borochov A, Faiman-Weinberg R, Gennis RB. 1984. Effects of pH and detergent on the kinetic and electrochemical properties of the purified cytochrome d complex of Escherichia coli. Biochim Biophys Acta 790:148-153.
    • (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
  • 155
    • 0027380681 scopus 로고
    • Sitedirected mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center
    • Thomas JW, Lemieux LJ, Alben JO, Gennis RB. 1993. Sitedirected mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center. Biochemistry 32:11173-11180.
    • (1993) Biochemistry , vol.32 , pp. 11173-11180
    • Thomas, J.W.1    Lemieux, L.J.2    Alben, J.O.3    Gennis, R.B.4
  • 156
    • 0027491552 scopus 로고
    • Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity
    • Thomas JW, Puustinen A, Alben JO, Gennis RB, Wikström M. 1993. Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity. Biochemistry 32:10923-10928.
    • (1993) Biochemistry , vol.32 , pp. 10923-10928
    • Thomas, J.W.1    Puustinen, A.2    Alben, J.O.3    Gennis, R.B.4    Wikström, M.5
  • 158
    • 33644848768 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli
    • Matsumoto Y, Murai M, Fujita D, Sakamoto K, Miyoshi H, Yoshida M, Mogi T. 2006. Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli. J Biol Chem 281:1905-1912.
    • (2006) J Biol Chem , vol.281 , pp. 1905-1912
    • Matsumoto, Y.1    Murai, M.2    Fujita, D.3    Sakamoto, K.4    Miyoshi, H.5    Yoshida, M.6    Mogi, T.7
  • 160
    • 33748115102 scopus 로고    scopus 로고
    • Asymmetrical evolution of cytochrome bd subunits
    • Hao W, Golding GB. 2006. Asymmetrical evolution of cytochrome bd subunits. J Mol Evol 62:132-142.
    • (2006) J Mol Evol , vol.62 , pp. 132-142
    • Hao, W.1    Golding, G.B.2
  • 161
    • 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
    • Zhang J, Hellwig P, Osborne JP, Gennis RB. 2004. 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 279:53980-53987.
    • (2004) J Biol Chem , vol.279 , pp. 53980-53987
    • Zhang, J.1    Hellwig, P.2    Osborne, J.P.3    Gennis, R.B.4
  • 162
    • 0026009165 scopus 로고
    • Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli
    • Oden KL, Gennis RB. 1991. Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli. J Bacteriol 173:6174-6183.
    • (1991) J Bacteriol , vol.173 , pp. 6174-6183
    • Oden, K.L.1    Gennis, R.B.2
  • 163
    • 0027212499 scopus 로고
    • Flow-flash study of the reaction between cytochrome bo and oxygen
    • Svensson M, Nilsson T. 1993. Flow-flash study of the reaction between cytochrome bo and oxygen. Biochemistry 32:5442-5447.
    • (1993) Biochemistry , vol.32 , pp. 5442-5447
    • Svensson, M.1    Nilsson, T.2
  • 164
    • 0038865077 scopus 로고
    • Oxygenated cytochrome bd from Escherichia coli can be converted into the oxidized form by lipophilic electron acceptors
    • (Translated from Biokhimiya 59:598-606, 1994.)
    • Borisov VB, Smirnova IA, Krasnosel'skaya IA, Konstantinov AA. 1994. Oxygenated cytochrome bd from Escherichia coli can be converted into the oxidized form by lipophilic electron acceptors. Biochemistry (Moscow) 59:437-443. (Translated from Biokhimiya 59:598-606, 1994.).
    • (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
  • 165
    • 0000613109 scopus 로고
    • The oxygenated complex of cytochrome d terminal oxidase: direct evidence for Fe-O2 coordination in a chlorin-containing enzyme by Resonance Raman spectroscopy
    • Kahlow MA, Loehr TM, Zuberi TM, Gennis RB. 1993. The oxygenated complex of cytochrome d terminal oxidase: direct evidence for Fe-O2 coordination in a chlorin-containing enzyme by Resonance Raman spectroscopy. J Am Chem Soc 115:5845-5846.
    • (1993) J Am Chem Soc , vol.115 , pp. 5845-5846
    • Kahlow, M.A.1    Loehr, T.M.2    Zuberi, T.M.3    Gennis, R.B.4
  • 166
    • 0024603308 scopus 로고
    • Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli
    • Lorence RM, Gennis RB. 1989. Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli. J Biol Chem 264:7135-7140.
    • (1989) J Biol Chem , vol.264 , pp. 7135-7140
    • Lorence, R.M.1    Gennis, R.B.2
  • 167
    • 0020627779 scopus 로고
    • The 650 nm chromophore in Escherichia coli is an 'oxy-' or oxygenated compound, not the oxidized form of cytochrome oxidase d: a hypothesis
    • Poole RK, Kumar C, Salmon I, Chance B. 1983. 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 129:1335-1344.
    • (1983) J Gen Microbiol , vol.129 , pp. 1335-1344
    • Poole, R.K.1    Kumar, C.2    Salmon, I.3    Chance, B.4
  • 169
    • 0019484649 scopus 로고
    • Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex
    • Alben JO, Moh PP, Fiamingo FG, Altschuld RA. 1981. Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex. Proc Natl Acad Sci USA 78:234-237.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 234-237
    • Alben, J.O.1    Moh, P.P.2    Fiamingo, F.G.3    Altschuld, R.A.4
  • 171
    • 0027308712 scopus 로고
    • Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation
    • WoodruffWH. 1993. Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation. J Bioenerg Biomembr 25:177-188.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 177-188
    • Woodruff, W.H.1
  • 174
    • 0027339969 scopus 로고
    • Ligand binding to the haem-copper binuclear catalytic site of cytochrome bo, a respiratory quinol oxidase from Escherichia coli
    • Ingledew WJ, Horrocks J, Salerno JC. 1993. Ligand binding to the haem-copper binuclear catalytic site of cytochrome bo, a respiratory quinol oxidase from Escherichia coli. Eur J Biochem 212:657-664.
    • (1993) Eur J Biochem , vol.212 , pp. 657-664
    • Ingledew, W.J.1    Horrocks, J.2    Salerno, J.C.3
  • 175
    • 0014681476 scopus 로고
    • Studies of the heme components of cytochrome c oxidase by EPR spectroscopy
    • Van Gelder BF, Beinert H. 1969. Studies of the heme components of cytochrome c oxidase by EPR spectroscopy. Biochim Biophys Acta 189:1-24.
    • (1969) Biochim Biophys Acta , vol.189 , pp. 1-24
    • Van Gelder, B.F.1    Beinert, H.2
  • 177
    • 0030851244 scopus 로고    scopus 로고
    • Comparison of the ligand-binding properties of native and copper-less cytochromes bo from Escherichia coli
    • Moody AJ, Mitchell R, Jeal AE, Rich PR. 1997. Comparison of the ligand-binding properties of native and copper-less cytochromes bo from Escherichia coli. Biochem J 324:743-752.
    • (1997) Biochem J , vol.324 , pp. 743-752
    • Moody, A.J.1    Mitchell, R.2    Jeal, A.E.3    Rich, P.R.4
  • 178
    • 0028054931 scopus 로고
    • Magnetic-circular-dichroism studies of Escherichia coli cytochrome bo identification of high-spin ferric, low-spin ferric and ferryl [Fe(IV)] forms of heme o
    • Cheesman MR, Watmough NJ, Gennis RB, Greenwood C, Thomson AJ. 1994. Magnetic-circular-dichroism studies of Escherichia coli cytochrome bo identification of high-spin ferric, low-spin ferric and ferryl [Fe(IV)] forms of heme o. Eur J Biochem 219:595-602.
    • (1994) Eur J Biochem , vol.219 , pp. 595-602
    • Cheesman, M.R.1    Watmough, N.J.2    Gennis, R.B.3    Greenwood, C.4    Thomson, A.J.5
  • 179
    • 0029961699 scopus 로고    scopus 로고
    • Infrared and EPR Studies on cyanide binding to the hemecopper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli
    • Tsubaki M, Mogi T, Hori H, Sato-Watanabe M, Anraku Y. 1996. Infrared and EPR Studies on cyanide binding to the hemecopper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli. J Biol Chem 271:4017-4022.
    • (1996) J Biol Chem , vol.271 , pp. 4017-4022
    • Tsubaki, M.1    Mogi, T.2    Hori, H.3    Sato-Watanabe, M.4    Anraku, Y.5
  • 180
    • 3843108952 scopus 로고    scopus 로고
    • 2+-C-N modes in heme-copper oxidases: a probe of the active site
    • 2+-C-N modes in heme-copper oxidases: a probe of the active site. Inorg Chem 43:4907-4910.
    • (2004) Inorg Chem , vol.43 , pp. 4907-4910
    • Pinakoulaki, E.1    Vamvouka, M.2    Varotsis, C.3
  • 182
    • 0027526880 scopus 로고
    • Fourier-transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: new evidence for a redox-linked conformational change at the binuclear site
    • Tsubaki M. 1993. Fourier-transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: new evidence for a redox-linked conformational change at the binuclear site. Biochemistry 32:174-182.
    • (1993) Biochemistry , vol.32 , pp. 174-182
    • Tsubaki, M.1
  • 183
    • 0027324414 scopus 로고
    • Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: WPR and Fourier transform infrared spectroscopic studies
    • Tsubaki M, Mogi T, Anraku Y, Hori H. 1993. Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: WPR and Fourier transform infrared spectroscopic studies. Biochemistry 32:6065-6072.
    • (1993) Biochemistry , vol.32 , pp. 6065-6072
    • Tsubaki, M.1    Mogi, T.2    Anraku, Y.3    Hori, H.4
  • 184
    • 0032963684 scopus 로고    scopus 로고
    • Fourier-transform infrared studies on azide-binding to the binuclear center of the Escherichia coli bo-type ubiquinol oxidase
    • Tsubaki M, Mogi T, Hori H. 1999. Fourier-transform infrared studies on azide-binding to the binuclear center of the Escherichia coli bo-type ubiquinol oxidase. FEBS Lett 449:191-195.
    • (1999) FEBS Lett , vol.449 , pp. 191-195
    • Tsubaki, M.1    Mogi, T.2    Hori, H.3
  • 185
    • 43249108452 scopus 로고    scopus 로고
    • Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity
    • (Translated from Biokhimiya 73:18-28, 2008.)
    • Borisov VB. 2008. Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity. Biochemistry (Moscow) 73:14-22. (Translated from Biokhimiya 73:18-28, 2008.).
    • (2008) Biochemistry (Moscow) , vol.73 , pp. 14-22
    • Borisov, V.B.1
  • 186
    • 0026067189 scopus 로고
    • Kinetics of the reactions of trioxodinitrate and nitrite ions with cytochrome d in Escherichia coli
    • Bonner FT, Hughes MN, Poole RK, Scott RI. 1991. Kinetics of the reactions of trioxodinitrate and nitrite ions with cytochrome d in Escherichia coli. Biochim Biophys Acta 1056:133-138.
    • (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
  • 188
    • 0021101983 scopus 로고
    • Nitrite, but not silver, ions induce spectral changes in Escherichia coli cytochrome d
    • Hubbard JAM, Hughes MN, Poole RK. 1983. Nitrite, but not silver, ions induce spectral changes in Escherichia coli cytochrome d. FEBS Lett 164:241-243.
    • (1983) FEBS Lett , vol.164 , pp. 241-243
    • Hubbard, J.A.M.1    Hughes, M.N.2    Poole, R.K.3
  • 189
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • Junemann S. 1997. Cytochrome bd terminal oxidase. Biochim Biophys Acta 1321:107-127.
    • (1997) Biochim Biophys Acta , vol.1321 , pp. 107-127
    • Junemann, S.1
  • 192
    • 0016277302 scopus 로고
    • Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli
    • Pudek MR, Bragg PD. 1974. Inhibition by cyanide of the respiratory chain oxidases of Escherichia coli. Arch Biochem Biophys 164:682-693.
    • (1974) Arch Biochem Biophys , vol.164 , pp. 682-693
    • Pudek, M.R.1    Bragg, P.D.2
  • 194
    • 0024284194 scopus 로고
    • Formation of the 680-nmabsorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form
    • Poole RK, Williams HD. 1988. Formation of the 680-nmabsorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form. FEBS Lett 231:243-246.
    • (1988) FEBS Lett , vol.231 , pp. 243-246
    • Poole, R.K.1    Williams, H.D.2
  • 195
    • 0029554848 scopus 로고
    • Peroxide complex of cytochrome bd: kinetics of generation and stability
    • Borisov V, Gennis R, Konstantinov AA. 1995. Peroxide complex of cytochrome bd: kinetics of generation and stability. Biochem Mol Biol Int 37:975-982.
    • (1995) Biochem Mol Biol Int , vol.37 , pp. 975-982
    • Borisov, V.1    Gennis, R.2    Konstantinov, A.A.3
  • 196
    • 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
    • Sun J, Osborne JP, Kahlow MA, Kaysser TM, Gennis RB, Loehr TM. 1995. 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 34:12144-12151.
    • (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
  • 197
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in Mitochondria
    • Wikström M. 1977. Proton pump coupled to cytochrome c oxidase in Mitochondria. Nature 266:271-273.
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.1
  • 198
    • 0024962043 scopus 로고
    • Cytochrome o(bo) is a proton pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen A, Finel M, Virkki M, Wikström M. 1989. Cytochrome o(bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett 249:163-167.
    • (1989) FEBS Lett , vol.249 , pp. 163-167
    • Puustinen, A.1    Finel, M.2    Virkki, M.3    Wikström, M.4
  • 199
    • 33745198219 scopus 로고    scopus 로고
    • Characterization of the exchangeable protons in the immediate vicinity of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli
    • Yap LL, Samoilova RI, Gennis RB, Dikanov SA. 2006. Characterization of the exchangeable protons in the immediate vicinity of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli. J Biol Chem 281:16879-16887.
    • (2006) J Biol Chem , vol.281 , pp. 16879-16887
    • Yap, L.L.1    Samoilova, R.I.2    Gennis, R.B.3    Dikanov, S.A.4
  • 200
    • 0034687655 scopus 로고    scopus 로고
    • Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo
    • Kobayashi K, Tagawa S, Mogi T. 2000. Transient formation of ubisemiquinone radical and subsequent electron transfer process in the Escherichia coli cytochrome bo. Biochemistry 39:15620-15625.
    • (2000) Biochemistry , vol.39 , pp. 15620-15625
    • Kobayashi, K.1    Tagawa, S.2    Mogi, T.3
  • 201
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • Belevich I, Verkhovsky MI, Wikström M. 2006. Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase. Nature 440:829-832.
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 203
    • 0027383797 scopus 로고
    • Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CObound forms of the bo3 and oo3 enzymes
    • Morgan JE, Verkhovsky MI, Puustinen A, Wikström M. 1993. Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CObound forms of the bo3 and oo3 enzymes. Biochemistry 32:11413-11418.
    • (1993) Biochemistry , vol.32 , pp. 11413-11418
    • Morgan, J.E.1    Verkhovsky, M.I.2    Puustinen, A.3    Wikström, M.4
  • 204
    • 0028219639 scopus 로고
    • Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site
    • Hallen S, Brzezinski P, Malmström BG. 1994. Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site. Biochemistry 33:1467-1472.
    • (1994) Biochemistry , vol.33 , pp. 1467-1472
    • Hallen, S.1    Brzezinski, P.2    Malmström, B.G.3
  • 205
    • 0025841838 scopus 로고
    • Internal electron transfer in cytochrome c oxidase: evidence for a rapid equilibrium between cytochrome a and the bimetallic site
    • Oliveberg M, Malmström BG. 1991. Internal electron transfer in cytochrome c oxidase: evidence for a rapid equilibrium between cytochrome a and the bimetallic site. Biochemistry 30:7053-7057.
    • (1991) Biochemistry , vol.30 , pp. 7053-7057
    • Oliveberg, M.1    Malmström, B.G.2
  • 207
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • Page CC, Moser CC, Dutton PL. 2003. Mechanism for electron transfer within and between proteins. Curr Opin Chem Biol 7:551-556.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 208
    • 0029861782 scopus 로고    scopus 로고
    • Kinetics of electron and proton transfer during the reaction of wild type and helix VI mutants of cytochrome bo3 with oxygen
    • Svensson-Ek M, Thomas JW, Gennis RB, Nilsson T, Brzezinski P. 1996. Kinetics of electron and proton transfer during the reaction of wild type and helix VI mutants of cytochrome bo3 with oxygen. Biochemistry 35:13673-13680.
    • (1996) Biochemistry , vol.35 , pp. 13673-13680
    • Svensson-Ek, M.1    Thomas, J.W.2    Gennis, R.B.3    Nilsson, T.4    Brzezinski, P.5
  • 211
    • 33750807024 scopus 로고    scopus 로고
    • Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase
    • Qin L, Hiser C, Mulichak A, Garavito RM, Ferguson-Miller S. 2006. Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc Natl Acad Sci USA 103:16117-16122.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16117-16122
    • Qin, L.1    Hiser, C.2    Mulichak, A.3    Garavito, R.M.4    Ferguson-Miller, S.5
  • 213
    • 0028607633 scopus 로고
    • The histidine cycle: a new model for proton translocation in the respiratory hemecopper oxidases
    • Morgan JE, Verkhovsky MI, Wikström M. 1994. The histidine cycle: a new model for proton translocation in the respiratory hemecopper oxidases. J Bioenerg Biomembr 26:599-608.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 599-608
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 215
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H. 1995. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 216
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of sitedirected mutations on time-resolved electrogenic intraprotein proton transfer
    • Konstantinov AA, Siletsky S, Mitchell D, Kaulen A, Gennis RB. 1997. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of sitedirected mutations on time-resolved electrogenic intraprotein proton transfer. Proc Natl Acad Sci USA 94:9085-9090.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 218
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikström M, Jasaitis A, Backgren C, Puustinen A, Verkhovsky MI. 2000. The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases. Biochim Biophys Acta 1459:514-520.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 220
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the hemecopper oxidase of Escherichia coli
    • Puustinen A, Wikstrom M. 1999. Proton exit from the hemecopper oxidase of Escherichia coli. Proc Natl Acad Sci USA 96:35-37.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikstrom, M.2
  • 221
    • 0030480043 scopus 로고    scopus 로고
    • The "ferrous-oxy" intermediate in the reaction of dioxygen with fully reduced cytochromes aa3 and bo3
    • Verkhovsky MI, Morgan JE, Puustinen A, Wikström M. 1996. The "ferrous-oxy" intermediate in the reaction of dioxygen with fully reduced cytochromes aa3 and bo3. Biochemistry 35:16241-16246.
    • (1996) Biochemistry , vol.35 , pp. 16241-16246
    • Verkhovsky, M.I.1    Morgan, J.E.2    Puustinen, A.3    Wikström, M.4
  • 222
    • 0032493345 scopus 로고    scopus 로고
    • Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase
    • Proshlyakov DA, Pressler MA, Babcock GT. 1998. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc Natl Acad Sci USA 95:8020-8025.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8020-8025
    • Proshlyakov, D.A.1    Pressler, M.A.2    Babcock, G.T.3
  • 223
    • 0033539479 scopus 로고    scopus 로고
    • Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase
    • Fabian M, Wong WW, Gennis RB, Palmer G. 1999. Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. Proc Natl Acad Sci USA 96:13114-13117.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13114-13117
    • Fabian, M.1    Wong, W.W.2    Gennis, R.B.3    Palmer, G.4
  • 224
    • 0028973405 scopus 로고
    • Identification of a "peroxy" intermediate in cytochrome bo3 of Escherichia coli
    • Morgan JE, Verkhovsky MI, Puustinen A, Wikström M. 1995. Identification of a "peroxy" intermediate in cytochrome bo3 of Escherichia coli. Biochemistry 34:15633-15637.
    • (1995) Biochemistry , vol.34 , pp. 15633-15637
    • Morgan, J.E.1    Verkhovsky, M.I.2    Puustinen, A.3    Wikström, M.4
  • 225
    • 0028167857 scopus 로고
    • Observation of the Fe-O2 and FeIV=0 stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli
    • Hirota S, Mogi T, Ogura T, Hirano T, Anraku Y, Kitagawa. 1994. Observation of the Fe-O2 and FeIV=0 stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli. FEBS Lett 352:67-70.
    • (1994) FEBS Lett , vol.352 , pp. 67-70
    • Hirota, S.1    Mogi, T.2    Ogura, T.3    Hirano, T.4    Anraku, Y.5    Kitagawa6
  • 226
    • 0028973038 scopus 로고
    • Reaction of cytochrome bo3 with oxygen: extra redox center(s) are present in the protein
    • Wang J, Rumbley J, Takahashi Y-C. Ching S, Gennis RB, Rousseau DL. 1995. Reaction of cytochrome bo3 with oxygen: extra redox center(s) are present in the protein. Biochemistry 34:15504-15511.
    • (1995) Biochemistry , vol.34 , pp. 15504-15511
    • Wang, J.1    Rumbley, J.2    Takahashi, Y.-C.3    Ching, S.4    Gennis, R.B.5    Rousseau, D.L.6
  • 227
    • 0027941055 scopus 로고
    • Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen
    • Orii Y, Mogi T, Kawasaki M, Anraku Y. 1994. Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen. FEBS Lett 352:151-154.
    • (1994) FEBS Lett , vol.352 , pp. 151-154
    • Orii, Y.1    Mogi, T.2    Kawasaki, M.3    Anraku, Y.4
  • 228
    • 0029959929 scopus 로고    scopus 로고
    • Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule
    • Puustinen A, Verkhovsky MI, Morgan JE, Belevich NP, Wikström M. 1996. Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. Proc Natl Acad Sci USA 93:1545-1548.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1545-1548
    • Puustinen, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Belevich, N.P.4    Wikström, M.5
  • 229
    • 0021682543 scopus 로고
    • Proton motive force is not obligatory for growth of Escherichia coli
    • Kinoshita N, Unemoto T, Kobayashi H. 1984. Proton motive force is not obligatory for growth of Escherichia coli. J Bacteriol 160:1074-1077.
    • (1984) J Bacteriol , vol.160 , pp. 1074-1077
    • Kinoshita, N.1    Unemoto, T.2    Kobayashi, H.3
  • 230
    • 0029880108 scopus 로고    scopus 로고
    • K+-dependent Na+ transport driven by respiration in Escherichia coli cells and membrane vesicles
    • Verkhovskaya ML, Verkhovsky MI, Wikström M. 1996. K+-dependent Na+ transport driven by respiration in Escherichia coli cells and membrane vesicles. Biochim Biophys Acta 1273:207-216.
    • (1996) Biochim Biophys Acta , vol.1273 , pp. 207-216
    • Verkhovskaya, M.L.1    Verkhovsky, M.I.2    Wikström, M.3
  • 231
    • 0019440530 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in Paracoccus denitrificans
    • van Verseveld HW, Krab K, Stouthamer AH. 1981. Proton pump coupled to cytochrome c oxidase in Paracoccus denitrificans. Biochim Biophys Acta 635:525-534.
    • (1981) Biochim Biophys Acta , vol.635 , pp. 525-534
    • van Verseveld, H.W.1    Krab, K.2    Stouthamer, A.H.3
  • 233
    • 33745602474 scopus 로고    scopus 로고
    • Elementary steps of proton translocation in the catalytic cycle of cytochrome oxidase
    • Verkhovsky MI, Belevich I, Bloch DA, Wikström M. 2006. Elementary steps of proton translocation in the catalytic cycle of cytochrome oxidase. Biochim Biophys Acta 1757:401-407.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 401-407
    • Verkhovsky, M.I.1    Belevich, I.2    Bloch, D.A.3    Wikström, M.4
  • 234
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén K, Gilderson G, Brzezinski P Ädelroth P. 2005. A mechanistic principle for proton pumping by cytochrome c oxidase. Nature 437:286-289.
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Brzezinski, P.3    Ädelroth, P.4
  • 235
    • 2442616154 scopus 로고    scopus 로고
    • Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating
    • Popovic DM, Stuchebrukhov AA. 2004. Proton pumping mechanism and catalytic cycle of cytochrome c oxidase: Coulomb pump model with kinetic gating. FEBS Lett 566:126-130.
    • (2004) FEBS Lett , vol.566 , pp. 126-130
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 236
    • 0142091718 scopus 로고    scopus 로고
    • Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase
    • Siegbahn PEM, Blomberg MRA, Blomberg ML. 2003. Theoretical study of the energetics of proton pumping and oxygen reduction in cytochrome oxidase. J Phys Chem B 107:10946-10955.
    • (2003) J Phys Chem B , vol.107 , pp. 10946-10955
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Blomberg, M.L.3
  • 237
    • 10644252589 scopus 로고    scopus 로고
    • Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase
    • Siletsky SA, Pawate AS, Weiss K, Gennis RB, Konstantinov AA. 2004. Transmembrane charge separation during the ferryl-oxo → oxidized transition in a nonpumping mutant of cytochrome c oxidase. J Biol Chem 279:52558-52565.
    • (2004) J Biol Chem , vol.279 , pp. 52558-52565
    • Siletsky, S.A.1    Pawate, A.S.2    Weiss, K.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 238
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • Wikström M, Verkhovsky MI. 2007. Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases. Biochim Biophys Acta 1767:1200-1214.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 239
    • 0021774196 scopus 로고
    • Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase
    • Koland JG, Miller MJ, Gennis RB. 1984. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry 23:445-453.
    • (1984) Biochemistry , vol.23 , pp. 445-453
    • Koland, J.G.1    Miller, M.J.2    Gennis, R.B.3
  • 240
    • 0000825077 scopus 로고
    • Reactions of cytochrome oxidase with oxygen and carbon monoxide
    • Gibson Q, Greenwood C. 1963. Reactions of cytochrome oxidase with oxygen and carbon monoxide. Biochem J 86:541-555.
    • (1963) Biochem J , vol.86 , pp. 541-555
    • Gibson, Q.1    Greenwood, C.2
  • 241
    • 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)
    • Dassa J, Fsihi H, Marck C, Dion M, Kieffer-Bontemps M, Boquet PL. 1991. 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 229:341-352.
    • (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
  • 242
    • 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
    • Atlung T, Brøndsted L. 1994. 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 176:5414-5422.
    • (1994) J Bacteriol , vol.176 , pp. 5414-5422
    • Atlung, T.1    Brøndsted, L.2
  • 243
    • 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
    • Brondsted L, Atlung T. 1996. 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 178:1556-1564.
    • (1996) J Bacteriol , vol.178 , pp. 1556-1564
    • Brondsted, L.1    Atlung, T.2
  • 244
    • 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
    • Sturr MG, Krulwich TA, Hicks DB. 1996. 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 176:1742-1749.
    • (1996) J Bacteriol , vol.176 , pp. 1742-1749
    • Sturr, M.G.1    Krulwich, T.A.2    Hicks, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.