Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH and near-micromolar oxygen: Oxygen affinity of NADH oxidase activity

Microbiology

Volumn 142, Issue 5, 1996, Pages 1141-1148

  Poole, Robert K ^a   Ioannidis, Nikolaos ^a,c   Orii, Yutaka ^b  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b KYOTO UNIVERSITY   (Japan)

^c INSTITUTE OF MATERIALS SCIENCE   (Greece)

Author keywords

Escherichia coli; Haemoglobin (bacterial); Hmp; Oxidase; Oxygen affinity

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; HEME; HEMOGLOBIN; OXYGEN; OXYHEMOGLOBIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

ARTICLE; ESCHERICHIA COLI; MICHAELIS CONSTANT; MOLECULAR WEIGHT; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029930852     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-5-1141     Document Type: Article

References (42)

1. Andrews, S. C., Shipley, D., Keen, J. N., Findlay, J. B. C., Harrison, P. M. & Guest, J. R. (1992). The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal shares homology with ferredoxin NADP+ reductases. FEBS Lett 302, 247-252.
2. Appleby, C. A. & Bergersen, F. J. (1980). Preparation and experimental use of leghaemoglobin. In Methods of Evaluating Biological Nitrogen Fixation, pp. 315-335, Edited by F. J. Bergersen. Chichester: John Wiley.
3. Boerman, S. & Webster, D. A. (1982). Control of heme content in Vitreoscilla by oxygen. J Gen Appl Microbiol 28, 35-43.
4. Chance, B., Legallais, V., Sorge, J. & Graham, N. (1975). A versatile time-sharing multichannel spectrophotometer, reflectometer, and fluorometer. Anal Biochem 66, 498-514.
5. Cooper, C. E., Ioannidis, N., D'mello, R. & Poole, R. K. (1994). Haem, flavin and oxygen interactions in Hmp, a flavohaemoglobin from Escherichia coli. Biochem Soc Trans 22, 709-713.
6. Cotter, P. A., Chepuri, V., Gennis, R. B. & Gunsalus, R. P. (1990). Cytochrome o (cyo ABCDE) and d (cyd AB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product. J Bacteriol 172, 6333-6338.
7. Cramm, R., Siddiqui, R. A. & Friedrich, B. (1994). Primary sequence and evidence for a physiological function of the flavohaemoprotein of Alcaligenes eutrophus. J Biol Chem 269, 7349-7354.
8. D'mello, R., Hill, S. & Poole, R. K. (1994). Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyleghaemoglobin and oxymyoglobin: cytochrome bd is a low-affinity oxidase. Microbiology 140, 1395-1402.
9. m values for oxygen are in the submicromolar range. J Bacteriol 177, 867-870.
10. D'mello, R., Hill, S. & Poole, R. K. (1996). The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition. Microbiology 142, (in press).
11. Eschenbrenner, M., Coves, J. & Fontecave, M. (1994). Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein. Biochem Biophys Res Commun 198, 127-131.
12. Favey, S., Labesse, G., Vouille, V. & Boccara, M. (1995). Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937. Microbiology 141, 863-871.
13. Gilles-González, M. A., González, G. & Perutz, M. F. (1995). Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron. Biochemistry 34, 232-236.
14. Hidalgo, E. & Demple, B. (1994). An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO J 13, 138-146.
15. Ioannidis, N., Cooper, C. E. & Poole, R. K. (1992). Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem J 288, 649-655.
16. Iwaasa, H., Takagi, T. & Shikama, K. (1992). Amino acid sequence of yeast hemoglobin. A two-domain structure. J Mol Biol 227, 948-954.
17. Jones, C. W. (1977). Aerobic respiratory systems in bacteria. In Microbial Energetics, pp. 23-59. Edited by B. A. Haddock & W. A. Hamilton. Cambridge: Cambridge University Press.
18. Karplus, P. A. & Bruns, C. M. (1994). Structure-function relation for ferredoxin reductase. J Bioenerg Biomembr 26, 89-99.
19. Khoroshilova, N., Beinert, H. & Kiley, P. J. (1995). Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc Natl Acad Sci USA 92, 2499-2503.
20. Khosla, C. & Bailey, J. E. (1988). Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli. Nature 331, 633-635.
21. Khosravi, M., Webster, D. A. & Stark, B. C. (1990). Presence of the bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain. Plasmid 24, 190-194.
22. Orii, Y. (1993). Immediate reduction of cytochrome c by photoexcited NADH: reaction mechanism as revealed by flow-flash and rapid-scan studies. Biochemistry 32, 11910-11914.
23. Orii, Y. & Webster, D. A. (1986). Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation. J Biol Chem 261, 3544-3547.
24. Orii, Y., Ioannidis, N. & Poole, R. K. (1992). The oxygenated flavohaemoglobin from Escherichia coli: evidence from photodissociation and rapid-scan studies for two kinetic and spectral forms. Biochem Biophys Res Commun 187, 94-100.
25. Oshino, R., Oshino, N., Chance, B. & Hagihara, B. (1973a). Studies on yeast hemoglobin. The properties of yeast hemoglobin and its physiological function in the cell. Eur J Biochem 35, 23-33.
26. Oshino, R., Asakura, T., Tajio, K., Oshino, N., Chance, B. & Hagihara, B. (1973b). Purification and molecular properties of yeast hemoglobin. Eur J Biochem 39, 581-590.
27. Perutz, M. F. (1986). A bacterial haemoglobin. Nature 322, 405.
28. Poole, R. K. (1994). Oxygen reactions with bacterial oxidases and globins : binding, reduction and regulation. Antonie Leeuwenhoek 65, 289-310.
29. Poole, R. K. & Chance, B. (1995). Oxidase names: to '3' or not to '3'? Microbiology 141, 752-753.
30. Poole, R. K., Ioannidis, N. & Orii, Y. (1994). Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide : evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing. Proc R Soc Lond B 255, 251-258.
31. Potts, M., Angeloni, S. V., Ebel, R. E. & Bassam, D. (1992). Myoglobin in a cyanobacterium. Science 256, 1690-1692.
32. Probst, I., Wolf, G. & Schlegel, H. G. (1979). An oxygen binding flavohemoprotein from Alcaligenes eutrophus. Biochim Biophys Acta 576, 471-478.
33. Rice, C. W. & Hempfling, W. P. (1978). Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J Bacteriol 134, 115-124.
34. Takagi, T. (1993). Hemoglobins from single-celled organisms. Curr Opin Struct Biol 3, 413-418.
35. 2-dependent gene regulation in facultatively anaerobic bacteria. Arch Microbiol 164, 81-90.
36. Vasudevan, S. G., Armarego, W. L. F., Shaw, D. C., Lilley, P. E. & Poole, R. K. (1991). Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12. Mol. Gen Genet 226, 49-58.
37. Vasudevan, S. G., Tang, P., Dixon, N. E. & Poole, R. K. (1995). Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli. FEMS Microbiol Lett 125, 219-224.
38. Wakabayashi, S., Matsubara, H. & Webster, D. A. (1986). Primary sequence of a dimeric haemoglobin from Vitreoscilla. Nature 322, 481-483.
39. Webster, D. A. (1987). Structure and function of bacterial hemoglobin and related proteins. In Advances in Inorganic Chemistry, vol. 7, pp. 245-265. Edited by G. L. Eichhorn & L. G. Marzilli. New York: Elsevier.
40. Webster, D. A. & Liu, C. Y. (1974). Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. J Biol Chem 249, 4257-4260.
41. Wood, P. M. (1984). Bacterial proteins with CO-binding b- or c-type haem. Functions and absorption spectroscopy. Biochim Biophys Acta 768, 293-317.
42. Zhu, H. & Riggs, A. F. (1992). Yeast flavohemoglobin is an ancient protein related to globins and a reductase family. Proc Natl Acad Sci USA 89, 5015-5019.