An unusual cytochrome o'-type cytochrome c oxidase in a Bacillus cereus cytochrome a3 mutant has a very high affinity for oxygen

Microbiology

Volumn 145, Issue 7, 1999, Pages 1563-1573

  Contreras, Martha L ^a   Escamilla, J Edgardo ^a   Del Arenal, I Patricia ^a   Davila J R ^b   D'mello, Rita ^c   Poole, Robert K ^d  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b BENEMÉRITA UNIVERSIDAD AUTÓNOMA DE PUEBLA   (Mexico)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

Bacillus cereus; Cytochrome aa3; Cytochrome o' like oxidase; Oxygen affinity; Sporulation

Indexed keywords

ASCORBIC ACID; BACTERIAL ENZYME; CARBON MONOXIDE; CYTOCHROME B; CYTOCHROME C; CYTOCHROME C OXIDASE; DITHIONITE; HEMOPROTEIN; N,N,N',N' TETRAMETHYL 1,4 PHENYLENEDIAMINE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

ARTICLE; BACILLUS CEREUS; BACTERIUM MUTANT; ENZYME ACTIVITY; NONHUMAN; OXYGEN AFFINITY; OXYGENATION; PRIORITY JOURNAL;

EID: 0032774445     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-145-7-1563     Document Type: Article

References (42)

1. Andreoli, A. J., Suehiro, S., Sakiyama, D., Takemoto, J., Vivanco, E., Lara, J. & Klute, M. C. (1973). Release and recovery of forespores from Bacillus cereus. J Bacteriol 115, 1159-1166.
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: Wiley.
3. 3 and o) from thermophilic bacterium PS3. Biochim Biophys Acta 766, 438-445.
4. Bergersen, F. J. & Turner, G. L. (1979). Systems utilizing oxygenated leghaemoglobin and myoglobin as sources of free dissolved oxygen at low concentrations for experiments with bacteria. Anal Biochem 96, 165-174.
5. 2-fixing bacteria grown in continuous culture. J Gen Microbiol 188, 235-252.
6. Calhoun, M. W., Thomas, J. W. & Gennis, R. B. (1994). The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci 19, 325-330.
7. Castor, L. N. & Chance, B. (1959). Photochemical determinations of the oxidases of bacteria. J Biol Chem 234, 1587-1592.
8. Chance, B., Graham, N. & Legallais, V. (1975a). Low temperature trapping methods for cytochrome oxidase intermediates. Anal Biochem 67, 552-579.
9. Chance, B., Legallais, V., Sorge, J. & Graham, N. (1975b). A versatile time-sharing multichannel spectrophotometer, reflectometer, and fluorometer. Anal Biochem 66, 498-514.
10. Ciccognani, D., Hughes, M. N. & Poole, R. K. (1992). Carbon monoxide-binding properties of the cytochrome bo quinol oxidase complex in Escherichia coli are changed by copper deficiency in continuous culture. FEMS Microbiol Lett 94, 1-6.
11. Clements, M. O., Watson, S. P., Poole, R. K. & Foster, S. J. (1999). CtaA of Staphylococcus aureus is required for starvation survival, recovery, and cytochrome biogenesis. J Bacteriol 181, 501-507.
12. Collier, R. E. (1957). An approach to synchronous growth for spore formation in Clostridium roseum. In Spores, pp. 10-17. Edited by H. O. Halvorson. Washington, DC : American Institute of Biological Sciences.
13. Cook, G. M., Loder, C., Søballe, B., Stafford, G. P., Membrillo-Hernández, J. & Poole, R. K. (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.
14. 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.
15. m values for oxygen are in the sub-micromolar range. J Bacteriol 177, 867-870.
16. 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, 755-763.
17. Del Arenal, I. P., Svlaeteorova, B. B., Contreras, M. L., Rangel, P., Dávila, J. R., Lledías, F. & Escamilla, J. E. (1997). Haem O and a putative cytochrome bo in a mutant of Bacillus cereus impaired in the synthesis of haem A. Arch Microbiol 167, 24-31.
18. Escamilla, J. E., Ramírez, R., Del Arenal, I. P. & Aranda, A. (1986). Respiratory systems of the Bacillus cereus mother cell and forespore. J Bacteriol 167, 544-550.
19. Escamilla, J. E., Ramírez, R., Del Arenal, I. P., Zarzoza, G. & Linares, V. (1987). Expression of cytochrome oxidases in Bacillus cereus: effects of oxygen tension and carbon source. J Gen Microbiol 133, 3549-3555.
20. 3-type cytochromes can be purified from the bacterium Bacillus cereus. Eur J Biochem 199, 761-768.
21. Gilmour, R. & Krulwich, T. A. (1997). Construction and characterisation of a mutant of alkaliphilic Bacillus firmus OF4 with a disrupted cta operon and purification of a novel cytochrome bd. J Bacteriol 179, 863-870.
22. Hanson, R.S., Srinivarsan, V.R. & Halvorson, H.O. (1963). Biochemistry of sporulation. J Bacteriol 85, 451-460.
23. Hill, J., Goswitz, V., Calhoun, M., Garcia-Horsman, J. A., Lemieux, L., Alben, J. O. & Gennis, R. B. (1992). Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product. Biochemistry 31, 11435-11440.
24. 3 and its replacement by cytochrome o in a mutant strain. FEMS Microbiol Lett 58, 277-282.
25. Jones, C. W. & Poole, R. K. (1985). Analysis of cytochromes. Methods Microbiol 18, 285-328.
26. Mitchell, D. M., Muller, J. D., Gennis, R. B. & Nienhaus, G. U. (1996). FTIR study of conformational substates in the CO adduct of cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry 35, 16782-16788.
27. Mogi, T., Saiki, K. & Anraku, Y. (1994). Biosynthesis and functional role of haem O and haem A. Mol Microbiol 14, 391-398.
28. Muntyan, M. S., Ludwig, B., Zickermann, I. & Starshinova, N. P. (1998). Role of copper during carbon monoxide binding to terminal oxidases. FEBS Lett 429, 216-220.
29. Poole, R. K. (1983). Bacteriol cytochrome oxidases : a structurally and functionally diverse group of electron transfer proteins. Biochim Biophys Acta 726, 205-243.
30. Poole, R. K. & Chance, B. (1995). Oxidase names: to '3' or not to '3'? Microbiology 141, 752-753.
31. Poole, R. K. & Hill, S. (1997). Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases. Biosci Rep 17, 303-317.
32. Poole, R. K., Waring, A. J. & Chance, B. (1979). The reaction of cytochrome o in Escherichia coli with oxygen. Low-temperature kinetic and spectral studies. Biochem J 184, 379-389.
33. Poole, R. K., Salmon, I. & Chance, B. (1994). The high-spin cytochrome o′ component of the cytochrome bo-type quinol oxidase in membranes from Escherichia coli: formation of the primary oxygenated species at low temperatures is characterized by a slow 'on' rate and low dissociation constant. Microbiology 140, 1027-1034.
34. 3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum. J Bacteriol 178, 1532-1538.
35. Puustinen, A. & Wikström, M. (1991). The heme groups of cytochrome o from Escherichia coli. Proc Natl Acad Sci USA 88, 6122-6126.
36. Sone, N. & Fujiwara, Y. (1991). Haem O can replace haem A in the active site of cytochrome c oxidase from thermophilic bacterium PS3. FEBS Lett 288, 154-158.
37. Sone, N., Kutoh, E. & Sato, K. (1990). A cytochrome o-type oxidase of thermophilic bacterium PS3 grown under air-limited conditions. J Biochem 107, 547-602.
38. Svensson, B., Lübben, M. & Hederstedt, L. (1993). Bacillus subtilis ctaA and ctaB function in heme A biosynthesis. Mol Microbiol 10, 193-201.
39. Taber, H. (1974). Isolation and properties of cytochrome a deficient mutants of Bacillus subtilis. J Gen Microbiol 81, 435-444.
40. Wood, P. M. (1984). Bacterial proteins with CO-binding b- or c-type haem. Functions and absorption spectroscopy. Biochim Biophys Acta 768, 293-317.
41. 3-type oxidases. Mol Microbiol 5, 2063-2072.
42. de Vrij, W., van den Burg, B. & Konings, W. N. (1987). Structural and potentiometric analysis of cytochromes from Bacillus subtilis. Eur J Biochem 166, 589-595.