In the respiratory chain of Escherichia coli cytochromes bd-I and bd-II are more sensitive to carbon monoxide inhibition than cytochrome bo 3

[1] L.K. Wareham H.M. Southam R.K. Poole Do nitric oxide, carbon monoxide and hydrogen sulfide really qualify as ‘gasotransmitters’ in bacteria? Biochem. Soc. Trans. 46 2018 1107 1118 L.K. Wareham, H.M. Southam, R.K. Poole, Do nitric oxide, carbon monoxide and hydrogen sulfide really qualify as 'gasotransmitters' in bacteria?, Biochem. Soc. Trans. 46 (2018) 1107-1118. [2] A. Verma D.J. Hirsch C.E. Glatt G.V. Ronnett S.H. Snyder Carbon monoxide: a putative neural messenger Science 259 1993 381 384 A. Verma, D.J. Hirsch, C.E. Glatt, G.V. Ronnett, S.H. Snyder, Carbon monoxide: a putative neural messenger, Science 259 (1993) 381-384. [3] J. Boczkowski J.J. Poderoso R. Motterlini CO-metal interaction: vital signaling from a lethal gas Trends Biochem. Sci. 31 2006 614 621 J. Boczkowski, J.J. Poderoso, R. Motterlini, CO-metal interaction: Vital signaling from a lethal gas, Trends Biochem. Sci. 31 (2006) 614-621. [4] N. Frankenberg-Dinkel Bacterial heme oxygenases Antioxid. Redox Signal. 6 2004 825 834 N. Frankenberg-Dinkel, Bacterial heme oxygenases, Antioxid. Redox. Signal. 6 (2004) 825-834. [5] M.D. Suits N. Jaffer Z. Jia Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193 J. Biol. Chem. 281 2006 36776 36782 M.D. Suits, N. Jaffer, Z. Jia, Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193, J. Biol. Chem. 281 (2006) 36776-36782. [6] M.U. Shiloh P. Manzanillo J.S. Cox Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection Cell Host Microbe 3 2008 323 330 M.U. Shiloh, P. Manzanillo, J.S. Cox, Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection, Cell Host Microbe 3 (2008) 323-330. [7] C.R. Scharn A.C. Collins V.R. Nair C.E. Stamm D.K. Marciano E.A. Graviss M.U. Shiloh Heme oxygenase-1 regulates inflammation and mycobacterial survival in human macrophages during Mycobacterium tuberculosis infection J. Immunol. 196 2016 4641 4649 C.R. Scharn, A.C. Collins, V.R. Nair, C.E. Stamm, D.K. Marciano, E.A. Graviss, M.U. Shiloh, Heme oxygenase-1 regulates inflammation and mycobacterial survival in human macrophages during Mycobacterium tuberculosis infection, J. Immunol. 196 (2016) 4641-4649. [8] L.C. Petersen The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase Biochim. Biophys. Acta 460 1977 299 307 L.C. Petersen, The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase, Biochim. Biophys. Acta 460 (1977) 299-307. [9] M.G. Mason P. Nicholls M.T. Wilson C.E. Cooper Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 103 2006 708 713 M.G. Mason, P. Nicholls, M.T. Wilson, C.E. Cooper, Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase, Proc. Natl. Acad. Sci. U S A 103 (2006) 708-713. [10] B. Wegiel R. Larsen D. Gallo B.Y. Chin C. Harris P. Mannam E. Kaczmarek P.J. Lee B.S. Zuckerbraun R. Flavell M.P. Soares L.E. Otterbein Macrophages sense and kill bacteria through carbon monoxide-dependent inflammasome activation J. Clin. Invest. 124 2014 4926 4940 B. Wegiel, R. Larsen, D. Gallo, B.Y. Chin, C. Harris, P. Mannam, E. Kaczmarek, P.J. Lee, B.S. Zuckerbraun, R. Flavell, M.P. Soares, L.E. Otterbein, Macrophages sense and kill bacteria through carbon monoxide-dependent inflammasome activation, J. Clin. Invest. 124 (2014) 4926-4940. [11] V.B. Borisov M.I. Verkhovsky Oxygen as acceptor EcoSal Plus 6 2015 V.B. Borisov, M.I. Verkhovsky, Oxygen as Acceptor, EcoSal Plus 6 (2015). [12] V. Chepuri L.J. Lemieux D.C.-T. Au R.B. Gennis The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa 3-type family of the cytochrome c oxidases J. Biol. Chem. 265 1990 11185 11192 V. Chepuri, L.J. Lemieux, D.C.-T. Au, R.B. Gennis, 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 (1990) 11185-11192. [13] M.W. Calhoun G. Newton R.B. Gennis E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli J. Bacteriol. 173 1991 1569 1570 M.W. Calhoun, G. Newton, R.B. Gennis, E. coli map. Physical map locations of genes encoding components of the aerobic respiratory chain of Escherichia coli, J. Bacteriol. 173 (1991) 1569-1570. [14] P.A. Cotter V. Chepuri R.B. Gennis R.P. Gunsalus Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product J. Bacteriol. 172 1990 6333 6338 P.A. Cotter, V. Chepuri, R.B. Gennis, R.P. Gunsalus, Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product, J. Bacteriol. 172 (1990) 6333-6338. [15] F.L. Sousa R.J. Alves M.A. Ribeiro J.B. Pereira-Leal M. Teixeira M.M. Pereira The superfamily of heme-copper oxygen reductases: types and evolutionary considerations Biochim. Biophys. Acta 1817 2012 629 637 F.L. Sousa, R.J. Alves, M.A. Ribeiro, J.B. Pereira-Leal, M. Teixeira, M.M. Pereira, The superfamily of heme-copper oxygen reductases: types and evolutionary considerations, Biochim. Biophys. Acta 1817 (2012) 629-637. [16] A. Puustinen M. Finel T. Haltia R.B. Gennis M. Wikstrom Properties of the two terminal oxidases of Escherichia coli Biochemistry 30 1991 3936 3942 A. Puustinen, M. Finel, T. Haltia, R.B. Gennis, M. Wikstrom, Properties of the two terminal oxidases of Escherichia coli, Biochemistry 30 (1991) 3936-3942. [17] J. Abramson S. Riistama G. Larsson A. Jasaitis M. Svensson-Ek L. Laakkonen A. Puustinen S. Iwata M. Wikstrom The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site Nat. Struct. Biol. 7 2000 910 917 J. Abramson, S. Riistama, G. Larsson, A. Jasaitis, M. Svensson-Ek, L. Laakkonen, A. Puustinen, S. Iwata, M. Wikstrom, The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site., Nat. Struct. Biol. 7 (2000) 910-917. [18] S.K. Choi L. Schurig-Briccio Z. Ding S. Hong C. Sun R.B. Gennis Location of the substrate binding site of the cytochrome bo 3 ubiquinol oxidase from Escherichia coli J. Am. Chem. Soc. 139 2017 8346 8354 S.K. Choi, L. Schurig-Briccio, Z. Ding, S. Hong, C. Sun, R.B. Gennis, Location of the substrate binding site of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, J. Am. Chem. Soc. 139 (2017) 8346-8354. [19] F. Melin S. Sabuncu S.K. Choi A. Leprince R.B. Gennis P. Hellwig Role of the tightly bound quinone for the oxygen reaction of cytochrome bo 3 oxidase from Escherichia coli FEBS Lett. 592 2018 3380 3387 F. Melin, S. Sabuncu, S.K. Choi, A. Leprince, R.B. Gennis, P. Hellwig, Role of the tightly bound quinone for the oxygen reaction of cytochrome bo3 oxidase from Escherichia coli, FEBS Lett. 592 (2018) 3380-3387. [20] J. Dassa H. Fsihi C. Marck M. Dion M. Kieffer-Bontemps P.L. Boquet A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA) Mol. Gen. Genet. 229 1991 341 352 J. Dassa, H. Fsihi, C. Marck, M. Dion, M. Kieffer-Bontemps, P.L. Boquet, A new oxygen-regulated operon in Escherichia coli comprises the genes for a putative third cytochrome oxidase and for pH 2.5 acid phosphatase (appA), Mol. Gen. Genet. 229 (1991) 341-352. [21] J. Hoeser S. Hong G. Gehmann R.B. Gennis T. Friedrich Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site FEBS Lett. 588 2014 1537 1541 J. Hoeser, S. Hong, G. Gehmann, R.B. Gennis, T. Friedrich, Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site, FEBS Lett. 588 (2014) 1537–1541. [22] R.J. Allen E.P. Brenner C.E. VanOrsdel J.J. Hobson D.J. Hearn M.R. Hemm Conservation analysis of the CydX protein yields insights into small protein identification and evolution BMC Genomics 15 2014 946 R.J. Allen, E.P. Brenner, C.E. VanOrsdel, J.J. Hobson, D.J. Hearn, M.R. Hemm, Conservation analysis of the CydX protein yields insights into small protein identification and evolution, BMC Genomics 15 (2014) 946. [23] L.V. Holyoake R.K. Poole M. Shepherd The CydDC family of transporters and their roles in oxidase assembly and homeostasis Adv. Microb. Physiol. 66 2015 1 53 L.V. Holyoake, R.K. Poole, M. Shepherd, The CydDC family of transporters and their roles in oxidase assembly and homeostasis, Adv. Microb. Physiol. 66 (2015) 1-53. [24] S. Alexeeva K.J. Hellingwerf M.J. Teixeira de Mattos Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions J. Bacteriol. 185 2003 204 209 S. Alexeeva, K.J. Hellingwerf, M.J. Teixeira de Mattos, Requirement of ArcA for redox regulation in Escherichia coli under microaerobic but not anaerobic or aerobic conditions, J. Bacteriol. 185 (2003) 204-209. [25] L. Brondsted T. Atlung Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli J. Bacteriol. 178 1996 1556 1564 L. Brondsted, T. Atlung, Effect of growth conditions on expression of the acid phosphatase (cyx-appA) operon and the appY gene, which encodes a transcriptional activator of Escherichia coli, J. Bacteriol. 178 (1996) 1556-1564. [26] T. Atlung L. Brondsted Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase J. Bacteriol. 176 1994 5414 5422 T. Atlung, L. Brondsted, Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase, J. Bacteriol. 176 (1994) 5414-5422. [27] R.K. Poole G.M. Cook Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation Adv. Microb. Physiol. 43 2000 165 224 R.K. Poole, G.M. Cook, Redundancy of aerobic respiratory chains in bacteria? Routes, reasons and regulation, Adv. Microb. Physiol. 43 (2000) 165–224. [28] W.J. Ingledew R.K. Poole The respiratory chains of Escherichia coli Microbiol. Rev. 48 1984 222 271 W.J. Ingledew, R.K. Poole, The respiratory chains of Escherichia coli, Microbiol. Rev. 48 (1984) 222-271. [29] S. Junemann Cytochrome bd terminal oxidase Biochim. Biophys. Acta 1321 1997 107 127 S. Junemann, Cytochrome bd terminal oxidase, Biochim. Biophys. Acta 1321 (1997) 107-127. [30] V.B. Borisov R.B. Gennis J. Hemp M.I. Verkhovsky The cytochrome bd respiratory oxygen reductases Biochim. Biophys. Acta 1807 2011 1398 1413 V.B. Borisov, R.B. Gennis, J. Hemp, M.I. Verkhovsky, The cytochrome bd respiratory oxygen reductases, Biochim. Biophys. Acta 1807 (2011) 1398-1413. [31] E. Forte V.B. Borisov J.B. Vicente A. Giuffrè Cytochrome bd and gaseous ligands in bacterial physiology Adv. Microb. Physiol. 71 2017 171 234 E. Forte, V.B. Borisov, J.B. Vicente, A. Giuffrè, Cytochrome bd and gaseous ligands in bacterial physiology, Adv. Microb. Physiol. 71 (2017) 171-234. [32] S.A. Siletsky V.B. Borisov M.D. Mamedov Photosystem II and terminal respiratory oxidases: molecular machines operating in opposite directions Front. Biosci. (Landmark Ed.) 22 2017 1379 1426 S.A. Siletsky, V.B. Borisov, M.D. Mamedov, Photosystem II and terminal respiratory oxidases: molecular machines operating in opposite directions, Front. Biosci. (Landmark Ed.) 22 (2017) 1379-1426. [33] A. Jasaitis V.B. Borisov N.P. Belevich J.E. Morgan A.A. Konstantinov M.I. Verkhovsky Electrogenic reactions of cytochrome bd Biochemistry 39 2000 13800 13809 A. Jasaitis, V.B. Borisov, N.P. Belevich, J.E. Morgan, A.A. Konstantinov, M.I. Verkhovsky, Electrogenic reactions of cytochrome bd, Biochemistry 39 (2000) 13800-13809. [34] V.B. Borisov R. Murali M.L. Verkhovskaya D.A. Bloch H. Han R.B. Gennis M.I. Verkhovsky Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode Proc. Natl. Acad. Sci. U. S. A. 108 2011 17320 17324 V.B. Borisov, R. Murali, M.L. Verkhovskaya, D.A. Bloch, H. Han, R.B. Gennis, M.I. Verkhovsky, Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode, Proc. Natl. Acad. Sci. USA 108 (2011) 17320–17324. [35] I. Belevich V.B. Borisov J. Zhang K. Yang A.A. Konstantinov R.B. Gennis M.I. Verkhovsky Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site Proc. Natl. Acad. Sci. U. S. A. 102 2005 3657 3662 I. Belevich, V.B. Borisov, J. Zhang, K. Yang, A.A. Konstantinov, R.B. Gennis, M.I. Verkhovsky, Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site, Proc. Natl. Acad. Sci. USA 102 (2005) 3657-3662. [36] I. Belevich V.B. Borisov M.I. Verkhovsky Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement J. Biol. Chem. 282 2007 28514 28519 I. Belevich, V.B. Borisov, M.I. Verkhovsky, Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement, J. Biol. Chem. 282 (2007) 28514-28519. [37] V.B. Borisov I. Belevich D.A. Bloch T. Mogi M.I. Verkhovsky 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 b 595/heme d active site Biochemistry 47 2008 7907 7914 V.B. Borisov, I. Belevich, D.A. Bloch, T. Mogi, M.I. Verkhovsky, 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 (2008) 7907–7914. [38] P. Sharma K.J. Hellingwerf M.J. Teixeira de Mattos M. Bekker Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth Appl. Environ. Microbiol. 78 2012 6908 6913 P. Sharma, K.J. Hellingwerf, M.J. Teixeira de Mattos, M. Bekker, Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth, Appl. Environ. Microbiol. 78 (2012) 6908-6913. [39] S. Safarian C. Rajendran H. Muller J. Preu J.D. Langer S. Ovchinnikov T. Hirose T. Kusumoto J. Sakamoto H. Michel Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases Science 352 2016 583 586 S. Safarian, C. Rajendran, H. Muller, J. Preu, J.D. Langer, S. Ovchinnikov, T. Hirose, T. Kusumoto, J. Sakamoto, H. Michel, Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases, Science 352 (2016) 583-586. [40] R. Murali R.B. Gennis Functional importance of glutamate-445 and glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli Biochim. Biophys. Acta 1859 2018 577 590 R. Murali, R.B. Gennis, Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli, Biochim. Biophys. Acta 1859 (2018) 577–590. [41] Y.H. Sun M.F. de Jong A.B. den Hartigh C.M. Roux H.G. Rolan R.M. Tsolis The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus Front. Cell. Infect. Microbiol. 2 2012 47 Y.H. Sun, M.F. de Jong, A.B. den Hartigh, C.M. Roux, H.G. Rolan, R.M. Tsolis, The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus, Front. Cell. Infect. Microbiol. 2 (2012) 47. [42] C.E. VanOrsdel S. Bhatt R.J. Allen E.P. Brenner J.J. Hobson A. Jamil B.M. Haynes A.M. Genson M.R. Hemm The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity J. Bacteriol. 195 2013 3640 3650 C.E. VanOrsdel, S. Bhatt, R.J. Allen, E.P. Brenner, J.J. Hobson, A. Jamil, B.M. Haynes, A.M. Genson, M.R. Hemm, The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity, J. Bacteriol. 195 (2013) 3640–3650. [43] H. Chen Q. Luo J. Yin T. Gao H. Gao Evidence for requirement of CydX in function but not assembly of the cytochrome bd oxidase in Shewanella oneidensis Biochim. Biophys. Acta 1850 2015 318 328 H. Chen, Q. Luo, J. Yin, T. Gao, H. Gao, Evidence for requirement of CydX in function but not assembly of the cytochrome bd oxidase in Shewanella oneidensis, Biochim. Biophys. Acta 1850 (2015) 318-328. [44] A. Lindqvist J. Membrillo-Hernandez R.K. Poole G.M. Cook Roles of respiratory oxidases in protecting Escherichia coli K12 from oxidative stress Antonie Van Leeuwenhoek 78 2000 23 31 A. Lindqvist, J. Membrillo-Hernandez, R.K. Poole, G.M. Cook, Roles of respiratory oxidases in protecting Escherichia coli K12 from oxidative stress, Antonie Van Leeuwenhoek 78 (2000) 23-31. [45] A. Giuffrè V.B. Borisov M. Arese P. Sarti E. Forte Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress Biochim. Biophys. Acta 1837 2014 1178 1187 A. Giuffrè, V.B. Borisov, M. Arese, P. Sarti, E. Forte, Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress, Biochim. Biophys. Acta 1837 (2014) 1178–1187. [46] V.B. Borisov E. Forte S.A. Siletsky P. Sarti A. Giuffrè Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition Biochim. Biophys. Acta 1847 2015 182 188 V.B. Borisov, E. Forte, S.A. Siletsky, P. Sarti, A. Giuffrè, Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition, Biochim. Biophys. Acta 1847 (2015) 182-188. [47] V.B. Borisov E. Forte S.A. Siletsky M. Arese A.I. Davletshin P. Sarti A. Giuffrè Cytochrome bd protects bacteria against oxidative and nitrosative stress: a potential target for next-generation antimicrobial agents Biochemistry-Moscow 80 2015 565 575 V.B. Borisov, E. Forte, S.A. Siletsky, M. Arese, A.I. Davletshin, P. Sarti, A. Giuffrè, Cytochrome bd protects bacteria against oxidative and nitrosative stress: a potential target for next-generation antimicrobial agents, Biochemistry-Moscow 80 (2015) 565-575. [48] E. Forte V.B. Borisov M. Falabella H.G. Colaco M. Tinajero-Trejo R.K. Poole J.B. Vicente P. Sarti A. Giuffrè The terminal oxidase cytochrome bd promotes sulfide-resistant bacterial respiration and growth Sci. Rep. 6 2016 23788 E. Forte, V.B. Borisov, M. Falabella, H.G. Colaco, M. Tinajero-Trejo, R.K. Poole, J.B. Vicente, P. Sarti, A. Giuffrè, The terminal oxidase cytochrome bd promotes sulfide-resistant bacterial respiration and growth, Sci. Rep. 6 (2016) 23788. [49] S. Korshunov K.R. Imlay J.A. Imlay The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide Mol. Microbiol. 101 2016 62 77 S. Korshunov, K.R. Imlay, J.A. Imlay, The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide, Mol. Microbiol. 101 (2016) 62-77. [50] V.B. Borisov Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity Biochemistry-Moscow 73 2008 14 22 V.B. Borisov, Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity, Biochemistry-Moscow 73 (2008) 14-22. [51] A. Puustinen M.I. Verkhovsky J.E. Morgan N.P. Belevich M. Wikstrom Reaction of the Escherichia coli quinol oxidase cytochrome bo 3 with dioxygen: the role of a bound ubiquinone molecule Proc. Natl. Acad. Sci. U. S. A. 93 1996 A. Puustinen, M.I. Verkhovsky, J.E. Morgan, N.P. Belevich, M. Wikstrom, Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: The role of a bound ubiquinone molecule, Proc. Natl. Acad. Sci. USA 93 (1996). [52] V. Borisov A.M. Arutyunyan J.P. Osborne R.B. Gennis A.A. Konstantinov Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands Biochemistry 38 1999 740 750 V. Borisov, A.M. Arutyunyan, J.P. Osborne, R.B. Gennis, A.A. Konstantinov, Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands, Biochemistry 38 (1999) 740-750. [53] M.R. Cheesman N.J. Watmough C.A. Pires R. Turner T. Brittain R.B. Gennis C. Greenwood A.J. Thomson Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide Biochem. J. 289 1993 709 718 M.R. Cheesman, N.J. Watmough, C.A. Pires, R. Turner, T. Brittain, R.B. Gennis, C. Greenwood, A.J. Thomson, Cytochrome bo from Escherichia coli: Identification of haem ligands and reaction of the reduced enzyme with carbon monoxide, Biochem. J. 289 (1993) 709-718. [54] S. Goutelle M. Maurin F. Rougier X. Barbaut L. Bourguignon M. Ducher P. Maire The Hill equation: a review of its capabilities in pharmacological modelling Fundam. Clin. Pharmacol. 22 2008 633 648 S. Goutelle, M. Maurin, F. Rougier, X. Barbaut, L. Bourguignon, M. Ducher, P. Maire, The Hill equation: a review of its capabilities in pharmacological modelling, Fundam. Clin. Pharmacol. 22 (2008) 633-648. [55] Y. Cheng W.H. Prusoff Relationship between the inhibition constant (K I ) and the concentration of inhibitor which causes 50 per cent inhibition (I 50) of an enzymatic reaction Biochem. Pharmacol. 22 1973 3099 3108 Y. Cheng, W.H. Prusoff, Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction, Biochem. Pharmacol. 22 (1973) 3099-3108. [56] M.G. Mason M. Shepherd P. Nicholls P.S. Dobbin K.S. Dodsworth R.K. Poole C.E. Cooper Cytochrome bd confers nitric oxide resistance to Escherichia coli Nat. Chem. Biol. 5 2009 94 96 M.G. Mason, M. Shepherd, P. Nicholls, P.S. Dobbin, K.S. Dodsworth, R.K. Poole, C.E. Cooper, Cytochrome bd confers nitric oxide resistance to Escherichia coli, Nat. Chem. Biol. 5 (2009) 94-96. [57] M. Bekker S. de Vries A. Ter Beek K.J. Hellingwerf M.J. de Mattos Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase J. Bacteriol. 191 2009 5510 5517 M. Bekker, S. de Vries, A. Ter Beek, K.J. Hellingwerf, M.J. de Mattos, Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase, J. Bacteriol. 191 (2009) 5510-5517. [58] R.M. Lorence J.G. Koland R.B. Gennis Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of “cytochrome a 1” as cytochrome b 595 Biochemistry 25 1986 2314 2321 R.M. Lorence, J.G. Koland, R.B. Gennis, 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 (1986) 2314-2321. [59] S. Junemann J.M. Wrigglesworth Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site J. Biol. Chem. 270 1995 16213 16220 S. Junemann, J.M. Wrigglesworth, Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site, J. Biol. Chem. 270 (1995) 16213-16220. [60] V.B. Borisov S.E. Sedelnikova R.K. Poole A.A. Konstantinov Interaction of cytochrome bd with carbon monoxide at low and room temperatures: evidence that only a small fraction of heme b 595 reacts with CO J. Biol. Chem. 276 2001 22095 22099 V.B. Borisov, S.E. Sedelnikova, R.K. Poole, A.A. Konstantinov, 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 (2001) 22095-22099. [61] V.B. Borisov U. Liebl F. Rappaport J.L. Martin J. Zhang R.B. Gennis A.A. Konstantinov M.H. Vos Interactions between heme d and heme b 595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy Biochemistry 41 2002 1654 1662 V.B. Borisov, U. Liebl, F. Rappaport, J.L. Martin, J. Zhang, R.B. Gennis, A.A. Konstantinov, M.H. Vos, Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy, Biochemistry 41 (2002) 1654-1662. [62] A.M. Arutyunyan J. Sakamoto M. Inadome Y. Kabashima V.B. Borisov Optical and magneto-optical activity of cytochrome bd from Geobacillus thermodenitrificans Biochim. Biophys. Acta 1817 2012 2087 2094 A.M. Arutyunyan, J. Sakamoto, M. Inadome, Y. Kabashima, V.B. Borisov, Optical and magneto-optical activity of cytochrome bd from Geobacillus thermodenitrificans, Biochim. Biophys. Acta 1817 (2012) 2087-2094. [63] S.A. Siletsky A.V. Dyuba D.A. Elkina M.V. Monakhova V.B. Borisov Spectral-kinetic analysis of recombination reaction of heme centers of bd-type quinol oxidase from Escherichia coli with carbon monoxide Biochemistry-Moscow 82 2017 1354 1366 S.A. Siletsky, A.V. Dyuba, D.A. Elkina, M.V. Monakhova, V.B. Borisov, Spectral-kinetic analysis of recombination reaction of heme centers of bd-type quinol oxidase from Escherichia coli with carbon monoxide, Biochemistry-Moscow 82 (2017) 1354-1366. [64] M.G. Sturr T.A. Krulwich D.B. Hicks Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4 J. Bacteriol. 178 1996 1742 1749 M.G. Sturr, T.A. Krulwich, D.B. Hicks, Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a Δcyo Δcyd strain complemented by genes from Bacillus firmus OF4, J. Bacteriol. 178 (1996) 1742-1749. [65] K. Kita K. Konishi Y. Anraku Terminal oxidases of Esherichia coli aerobic respiratory chain. I. Purification and properties of cytochrome b 562-o complex from cells in the early exponential phase of aerobic growth J. Biol. Chem. 259 1984 3368 3374 K. Kita, K. Konishi, Y. Anraku, Terminal Oxidases of Esherichia 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 (1984) 3368-3374. [66] K. Matsushita L. Patel H.R. Kaback Cytochrome o type oxidase from Escherichia coli. Characterization of the enzyme and mechanism of electrochemical proton gradient generation Biochemistry 23 1984 4703 4714 K. Matsushita, L. Patel, H.R. Kaback, Cytochrome o Type Oxidase from Escherichia coli. Characterization of the Enzyme and Mechanism of Electrochemical Proton Gradient Generation, Biochemistry 23 (1984) 4703-4714. [67] A. Puustinen M. Wikstrom The heme groups of cytochrome o from Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 88 1991 6122 6126 A. Puustinen, M. Wikstrom, The Heme Groups of Cytochrome o from Escherichia coli, Proc. Natl. Acad. Sci. USA 88 (1991) 6122-6126. [68] H.E. Jesse T.L. Nye S. McLean J. Green B.E. Mann R.K. Poole Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or bo″ to inhibition by the carbon monoxide-releasing molecule, CORM-3: N-acetylcysteine reduces CO-RM uptake and inhibition of respiration Biochim. Biophys. Acta 1834 2013 1693 1703 H.E. Jesse, T.L. Nye, S. McLean, J. Green, B.E. Mann, R.K. Poole, Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or bo” to inhibition by the carbon monoxide-releasing molecule, CORM-3: N-acetylcysteine reduces CO-RM uptake and inhibition of respiration, Biochim. Biophys. Acta 1834 (2013) 1693–1703. [69] J.G. Lindsay D.F. Wilson Reaction of cytochrome c oxidase with CO: involvement of the invisible copper FEBS Lett. 48 1974 45 49 J.G. Lindsay, D.F. Wilson, Reaction of cytochrome c oxidase with CO: involvement of the invisible copper, FEBS Lett. 48 (1974) 45-49. [70] S. Junemann J.M. Wrigglesworth P.R. Rich Effects of decyl-aurachin D and reversed electron transfer in cytochrome bd Biochemistry 36 1997 9323 9331 S. Junemann, J.M. Wrigglesworth, P.R. Rich, Effects of decyl-aurachin D and reversed electron transfer in cytochrome bd, Biochemistry 36 (1997) 9323-9331. [71] M.H. Vos V.B. Borisov U. Liebl J.L. Martin A.A. Konstantinov Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: a di-heme active site? Proc. Natl. Acad. Sci. U. S. A. 97 2000 1554 1559 M.H. Vos, V.B. Borisov, U. Liebl, J.L. Martin, A.A. Konstantinov, Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?, Proc. Natl. Acad. Sci. USA 97 (2000) 1554-1559. [72] F. Rappaport J. Zhang M.H. Vos R.B. Gennis V.B. Borisov Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy Biochim. Biophys. Acta 1797 2010 1657 1664 F. Rappaport, J. Zhang, M.H. Vos, R.B. Gennis, V.B. Borisov, Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy, Biochim. Biophys. Acta 1797 (2010) 1657–1664. [73] S.A. Siletsky A.A. Zaspa R.K. Poole V.B. Borisov Microsecond time-resolved absorption spectroscopy used to study CO compounds of cytochrome bd from Escherichia coli PLoS One 9 2014 e95617 S.A. Siletsky, A.A. Zaspa, R.K. Poole, V.B. Borisov, Microsecond time-resolved absorption spectroscopy used to study CO compounds of cytochrome bd from Escherichia coli, PLoS One 9 (2014) e95617. [74] V.B. Borisov E. Forte P. Sarti M. Brunori A.A. Konstantinov A. Giuffrè Redox control of fast ligand dissociation from Escherichia coli cytochrome bd Biochem. Biophys. Res. Commun. 355 2007 97 102 V.B. Borisov, E. Forte, P. Sarti, M. Brunori, A.A. Konstantinov, A. Giuffrè, Redox control of fast ligand dissociation from Escherichia coli cytochrome bd, Biochem. Biophys. Res. Commun. 355 (2007) 97-102. [75] B.C. Hill J.J. Hill R.B. Gennis The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli Biochemistry 33 1994 15110 15115 B.C. Hill, J.J. Hill, R.B. Gennis, The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli, Biochemistry 33 (1994) 15110-15115. [76] R. Mitchell A.J. Moody P.R. Rich Cyanide and carbon monoxide binding to the reduced form of cytochrome bo from Escherichia coli Biochemistry 34 1995 7576 7585 R. Mitchell, A.J. Moody, P.R. Rich, Cyanide and Carbon Monoxide Binding to the Reduced Form of Cytochrome bo from Escherichia coli, Biochemistry 34 (1995) 7576-7585. [77] D.D. Lemon M.W. Calhoun R.B. Gennis W.H. Woodruff The gateway to the active site of heme-copper oxidases Biochemistry 32 1993 11953 11956 D.D. Lemon, M.W. Calhoun, R.B. Gennis, W.H. Woodruff, The gateway to the active site of heme-copper oxidases, Biochemistry 32 (1993) 11953-11956. [78] Q. Gibson C. Greenwood Reactions of cytochrome oxidase with oxygen and carbon monoxide Biochem. J. 86 1963 541 555 Q. Gibson, C. Greenwood, Reactions of cytochrome oxidase with oxygen and carbon monoxide, Biochem. J. 86 (1963) 541-555. [79] A.L. Tsai V. Berka E. Martin J.S. Olson A “sliding scale rule” for selectivity among NO, CO, and O2 by heme protein sensors Biochemistry 51 2012 172 186 A.L. Tsai, V. Berka, E. Martin, J.S. Olson, A "sliding scale rule" for selectivity among NO, CO, and O2 by heme protein sensors, Biochemistry 51 (2012) 172-186. [80] H.M. Southam T.W. Smith R.L. Lyon C. Liao C.R. Trevitt L.A. Middlemiss F.L. Cox J.A. Chapman S.F. El-Khamisy M. Hippler M.P. Williamson P.J.F. Henderson R.K. Poole A thiol-reactive Ru(II) ion, not CO release, underlies the potent antimicrobial and cytotoxic properties of CO-releasing molecule-3 Redox Biol. 18 2018 114 123 H.M. Southam, T.W. Smith, R.L. Lyon, C. Liao, C.R. Trevitt, L.A. Middlemiss, F.L. Cox, J.A. Chapman, S.F. El-Khamisy, M. Hippler, M.P. Williamson, P.J.F. Henderson, R.K. Poole, A thiol-reactive Ru(II) ion, not CO release, underlies the potent antimicrobial and cytotoxic properties of CO-releasing molecule-3, Redox Biol. 18 (2018) 114-123. [81] L.K. Wareham R. Begg H.E. Jesse J.W. Van Beilen S. Ali D. Svistunenko S. McLean K.J. Hellingwerf G. Sanguinetti R.K. Poole Carbon monoxide gas is not inert, but global, in its consequences for bacterial gene expression, iron acquisition, and antibiotic resistance Antioxid. Redox Signal. 24 2016 1013 1028 L.K. Wareham, R. Begg, H.E. Jesse, J.W. Van Beilen, S. Ali, D. Svistunenko, S. McLean, K.J. Hellingwerf, G. Sanguinetti, R.K. Poole, Carbon Monoxide Gas Is Not Inert, but Global, in Its Consequences for Bacterial Gene Expression, Iron Acquisition, and Antibiotic Resistance, Antioxid. Redox. Signal. 24 (2016) 1013-1028.