The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition

References

1. Appleby C.A., Bergersen F.J. Methods of Evaluating Etiological Nitrogen Fixation 1980 Edited by Bergersen F.J. Chichester: John Wiley; pp 315–335
   [Google Scholar]
2. Bergersen F.J., Turner G.L. Measurements of components of proton motive force and related parameters in steady state, microaerobic conditions. J Microbiol Methods 1985; 4:13–23
   [Google Scholar]
3. Berzofsky J.A., Peisach J., Blumberg W.E. Sulphaem proteins. 1. Optical and magnetic properties of sulfmyoglobin and its derivatives. J Biol Chem 1971; 246:3367–3377
   [Google Scholar]
4. Castor L.N., Chance B. Photochemical determinations of the oxidases of bacteria. J Biol Chem 1959; 234:1587–1592
   [Google Scholar]
5. Chance B., Legallais V., Sorge J., Graham N. A versatile time-sharing multichannel spectrophotometer, reflectometer and fluorometer. Anal B'tochem 1975; 66:498–514
   [Google Scholar]
6. Cleland W.W. aaaa. In The Enzymes 1970 Edited by Boyer P.D. New York: Academic Press; 2 pp 1–65
   [Google Scholar]
7. Cotter P.A., Chepuri V., Gennis R.B., Gunsalus R.P. Cytochrome o (cyoABCDE) and d (cjdAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH and the fnr gene product. J Bacteriol 1990; 172:6333–6338
   [Google Scholar]
8. D'mello R., Hill S., Poole R.K. Determination of the oxygen affinities of terminal oxidases in A^otobacter vinelandii using the deoxygenation of oxyleghaemoglobin and oxymyoglobin: cytochrome bd is a low-affinity oxidase. Microbiology 1994a; 140:1395–1402
   [Google Scholar]
9. D'mello R., Palmer S., Hill S., Poole R.K. The cytochrome bd terminal oxidase of Azotobacter vinelandii: low temperature photodissociation spectrophotometry reveals reactivity of cytochromes ¿595 and d with both carbon monoxide and oxygen. FEMS Microbiol Lett 1994b; 121:115–120
   [Google Scholar]
10. D'mello R., Hill S., Poole R.K. The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghaemoglobin and oxymyoglobin: Km values for oxygen are in the submicromolar range. J Bacteriol 1995; 177:867–870
    [Google Scholar]
11. Edwards C., Beer S., Siviram A., Chance B. Photochemical action spectra of bacterial a- and o-type oxidases using a dye laser. FEBS Lett 1981; 128:205–207
    [Google Scholar]
12. Fu H.-A., luchi S., Lin E.C.C. The requirement of ArcA and Fnr for peak expression of the cyd operon in Escherichia coli under microaerobic conditions. Mol & Gen Genet 1991; 226:209–213
    [Google Scholar]
13. Gibson Q.H. Hemoproteins, ligands and quanta. J Biol Chem 1989; 264:20155–20158
    [Google Scholar]
14. Guerin M.G., Camougrand N.M. Partitioning of electron flux between the respiratory chains of the yeast Candida parapsilosis: parallel working of the two chains. Biochim Biophjs Acta 1994; 1184:111–117
    [Google Scholar]
15. Hill J.J., Alben J.O., Gennis R.B. Spectroscopic evidence for a haem-haem binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc Natl Acad Sci USA 1993; 90:5863–5867
    [Google Scholar]
16. Hill S., Viollet S., Smith A.T., Anthony C. Roles for enteric d-type cytochrome oxidase in N2 fixation and micro-aerobiosis. J Bacterial 1990; 172:2071–2078
    [Google Scholar]
17. Ingledew W.J., Saraste M. The reaction of cytochrome cd1 with oxygen and peroxides. Biochem Soc Trans 1979; 7:166–168
    [Google Scholar]
18. Kahlow M.A., Zuberi T.M., Gennis R.B., Loehr T.M. Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy. Biochemistry 1991; 30:11485–11489
    [Google Scholar]
19. Kelly M.J.S., Poole R.K., Yates M.G., Kennedy C. Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Agotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air. J Bacteriol 1990; 172:6010–6019
    [Google Scholar]
20. Kita K., Konishi K., Anraku Y. Terminal oxidases of Escherichia coli aerobic respiratory chain. II. Purification and properties of cytochrome bb5S-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems. J Biol Chem 1984; 259:3375–3381
    [Google Scholar]
21. Kitts C.L., Ludwig R.A. Azorhizobium caulinodans respires with at least four terminal oxidases. J Bacteriol 1994; 176:886–895
    [Google Scholar]
22. Kolonay J.F., Moshiri F., Gennis R.B., Kaysser T.M., Maier R.J. Purification and characterization of the cytochrome bd complex from Azotobacter vinelandii: comparison to the complex from Escherichia coli. J Bacteriol 1994; 176:4177–4181
    [Google Scholar]
23. Krasnoselskaya I., Arutjunjan A.M., Smirnova I., Gennis R.B., Konstantinov A.A. Cyanide-reactive sites in cytochrome bd complex from Escherichia coli. FEBS Lett 1993; 327:279–283
    [Google Scholar]
24. Lemieux L.J., Calhoun M.W., Thomas J.W., Ingledew W.J., Gennis R.B. Determination of the ligands of the low-spin haem of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis. J Biol Chem 1992; 267:2105–2113
    [Google Scholar]
25. Longmuir I.S. Respiration rate of bacteria as a function of oxygen concentration. Biochem J 1954; 57:81–87
    [Google Scholar]
26. Lundsgaard J.S., Grolund J., Degn H. Error in oxygen measurements in open systems owing to oxygen consumption in the unstirred layer. Biotechnol Bioeng 1978; 20:809–819
    [Google Scholar]
27. Maniatis T., Fritsch E.F., Sambrook J. Molecular Cloning: a Laboratory Manual 1982 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
28. Markwell M.A.K., Haas S.M., Bieber L.L., Tolbert N.E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 1978; 87:206–210
    [Google Scholar]
29. Paget T.A., Jarroll E.L., Manning P., Lindmark D.G., Lloyd D. Respiration in the cysts and trophozoites of Giardia muris. J Gen Microbiol 1989; 135:145–154
    [Google Scholar]
30. Poole R.K. Bacterial cytochrome oxidases: a structurally and functionally diverse group of electron-transfer proteins. Biochim Biophys Acta 1983; 726:205–243
    [Google Scholar]
31. Poole R.K. Oxygen reactions with bacterial oxidases and globins : binding, reduction and regulation. Antonie Leeuwenhoek 1994; 65:289–310
    [Google Scholar]
32. Poole R.K., Chance B. The reaction of cytochrome o in Escherichia coli K12 with oxygen. Evidence for a spectrally and kinetically distinct cytochrome o in cells from oxygen-limited cultures. J Gen Microbiol 1981; 126:277–287
    [Google Scholar]
33. Poole R.K., Chance B. Oxidase names : to ‘ 3 ’ or not to ‘3’. Microbiology 1995; 141:752–753
    [Google Scholar]
34. Poole R.K., Williams H.D. Proposal that the function of the membrane-bound cytochrome ax-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d. FEBS Lett 1987; 217:49–52
    [Google Scholar]
35. Poole R.K., Waring A.J., Chance B. The reaction of cytochrome o in Escherichia coli with oxygen. Biochem J 1979; 184:379–389
    [Google Scholar]
36. Poole R.K., Scott R.I., Chance B. The light-reversible binding of carbon monoxide to cytochrome ax in Escherichia coli K12. J Gen Microbiol 1981; 125:431–438
    [Google Scholar]
37. Poole R.K., Sivaram A., Salmon I., Chance B. Photolysis at very low temperature of CO-ligated cytochrome oxidase (cytochrome d) in oxygen-limited Escherichia coli. FEBS Lett 1982a; 141:237–241
    [Google Scholar]
38. Poole R.K., Baines B.S., Hubbard J.A.M., Hughes M.N., Campbell N.J. Resonance Raman spectroscopy of an oxygenated intermediate species of cytochrome oxidase d from Escherichia coli. FEBS Lett 1982b; 150:147–149
    [Google Scholar]
39. Poole R.K., Kumar C., Salmon I., Chance B. The 650 nm chromophore in Escherichia coli is an oxygenated compound, not the oxidized form of cytochrome d oxidase: an hypothesis. J Gen Microbiol 1983a; 129:1335–1344
    [Google Scholar]
40. Poole R.K., Salmon I., Chance B. The reaction with oxygen of cytochrome oxidase (cytochrome d) in Escherichia coli K12: optical studies of intermediate species and cytochrome b oxidation at subzero temperatures. J Gen Microbiol 1983b; 129:1345–1355
    [Google Scholar]
41. Poole R.K., Williams H.D., Downie J.A., Gibson F. Mutations affecting the cytochrome ¿/-containing oxidase complex of Escherichia coli K12: identification and mapping of a fourth locus, cydD. J Gen Microbiol 1989; 135:1865–1874
    [Google Scholar]
42. Puustinen A., Finel M., Haltia T., Gennis R.B., Wikstrom M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry 1991; 30:3936–3942
    [Google Scholar]
43. Rice C.W., Hempfling W.P. Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J Bacteriol 1978; 134:115–124
    [Google Scholar]
44. Rothery R.A., Houston A.M., Ingledew W.J. The respiratory chain of anaerobically grown Escherichia coli: reactions with nitrite and oxygen. J Gen Microbiol 1987; 133:3247–3255
    [Google Scholar]
45. Smith A., Hill S., Anthony C. The purification, characterization and role of the ¿/-type cytochrome oxidase of Klebsiella pneumoniae during nitrogen fixation. J Gen Microbiol 1990; 136:171–180
    [Google Scholar]
46. Timkovitch R., Cork M.S., Gennis R.B., Johnson P.Y. Proposed structure of haem D, a prosthetic group of bacterial terminal oxidases. J Am Chem Soc 1985; 107:6069–6075
    [Google Scholar]
47. Wood P.M. Bacterial proteins with CO-binding b- or c-type haem; functions and absorption spectroscopy. Biochim Biophys Acta 1984; 768:293–317
    [Google Scholar]