Type 2 Cu2+ in pMMO from Methylomicrobium album BG8

Biophysical Journal

Volumn 76, Issue 4, 1999, Pages 2223-2229

  Yuan, Hua ^a,c   Collins, Mary Lynne Perille ^b   Antholine, William E ^a  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

^b UNIVERSITY OF WISCONSIN MILWAUKEE   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COPPER ION; ENZYME; METHANE MONOOXYGENASE; NITROGEN; PEPTIDE; COPPER; OXYGENASE; PEPTIDE FRAGMENT;

AMINO ACID ANALYSIS; ARTICLE; BACTERIAL GROWTH; CELL MEMBRANE; CHEMICAL BINDING; CONCENTRATION (PARAMETERS); ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME ANALYSIS; MAGNETIC FIELD; NONHUMAN; PEPTIDE SYNTHESIS; PROTEIN ANALYSIS; PROTEIN BINDING; AMINO ACID SEQUENCE; BINDING SITE; BIOPHYSICS; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; METHYLOCOCCACEAE; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; BINDING SITES; BIOPHYSICS; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; METHYLOCOCCACEAE; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NITROGEN; OXYGENASES; PEPTIDE FRAGMENTS;

EID: 0032586758     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77378-9     Document Type: Article

References (27)

1. Anthony, C. 1986. Bacterial oxidation of methane and methanol. Adv. Microb. Physiol. 27:113-209.
2. Brantner, C. A., L. A. Buchholz, C. C. Remsen, and M. L. P. Collins. 1997. Intracytoplasmic membrane formation in Methylomicrobium album BG8 is stimulated by copper in the growth medium. Can. J. Microbiol. 43:672-676.
3. Chan, S. I., H.-H. T. Nguyen, A. K. Shiemke, and M. E. Lidstrom. 1993. The copper ions in the membrane-associated methane monooxygenase. In Bioinorganic Chemistry of Copper. K. Karlin and Z. Tueklar, editors. Chapman and Hall, New York. 184-195.
4. Collins, M. L. P., L. A. Buchholz, and C. C. Remsen. 1991. Effect of copper on Methylomonas albus BG8. Appl. Environ. Microbiol. 57: 1261-1264.
5. Elliott, S. J., D. W. Randall, R. D. Britt, and S. I. Chan. 1998. Pulsed EPR studies of particulate methane monooxygenase from Methylococcus capsulatus (Bath): evidence for histidine ligation. J. Am. Chem. Soc. 120:3247-3248.
6. Elliott, S. J., M. Zhu, L. Tso, H.-H. T. Nguyen, J. H.-K. Yip, and S. I. Chan. 1997. Regio- and stereoselectivity of particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Am. Chem. Soc. 119: 9949-9955.
7. Halfen, J. A., S. Mahapatra, E. C. Wilkinson, S. Kaderli, V. G. Young, L. Que, A. D. Zuberbuhler, and W. B. Tolman. 1996. Reversible cleavage and formation of the dioxygen O-O bond within a dicopper complex. Science. 271:1397-1400.
8. Hanson, R. S., and T. E. Hanson. 1996. Methanotrophic bacteria. Microbiol. Rev. 60:439-471.
9. Hanson, R. S., A. I. Netrusov, and K. Tsuji. 1991. The obligate methanotrophic bacteria Methylococcus, Methylomonas, and Methylosinus. In The Procaryotes. A. Bolows, H. G. Truper, M. Dworkin, and K. Schliefer, editors. Springer Verlag, New York. 2350-2364.
10. Lipscomb, J. D. 1994. Biochemistry of the soluble methane monooxygenase. Annu. Rev. Microbiol. 48:371-399.
11. Mahapatra, S., J. A. Halfen, E. C. Wilkinson, G. Pan, X. Wang, V. G. Young, C. J. Cramer, L. Que, and W. B. Tolman. 1996. Structural, spectroscopic, and theoretical characterization of bis(μ-oxo) dicopper complexes, novel intermediates in copper-mediated dioxygen activation. J. Am. Chem. Soc. 118:11555-11574.
12. Maurice, A. M. 1980. Ph.D. thesis. University of Illinois, Urbana, IL.
13. Murrell, J. C., and A. J. Holmes. 1996. Molecular biology of particulate methane monooxygenase. In Microbial Growth on C Compounds. M. E. Lidstrom and F. R. Tabita, editors. Kluwer Academic Publishers, Amsterdam. 133-140.
14. Nguyen, H.-H. T., S. J. Elliott, J. H.-K. Yip, and S. I. Chan. 1998. The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. J. Biol. Chem. 273:7957-7966.
15. Nguyen, H.-H. T., K. H. Nakagawa, B. Hedman, S. J. Elliott, M. E. Lidstrom, K. D. Hodgson, S. I. Chan. 1996. X-ray absorption and EPR studies on the copper ions associated with particulate methane monooxygenase from Methylococcus capsulatus (Bath): Cu(I) ions and their implications. J. Am. Chem. Soc. 118:12766-12776.
16. Nguyen, H.-H. T., A. K. Shiemke, L. J. Jacobs, B. J. Hales, M. E. Lidstrom, and S. I. Chan. 1994. The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 269:14995-15005.
17. Nigles, M. J. 1979. Ph.D. thesis. University of Illinois, Urbana, IL.
18. Prior, S. D., and H. Dalton. 1985. The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells of Methylococcus capsulatus (Bath). J. Gen. Microbiol. 131:155-163.
19. Rakhit, G., W. E. Antholine, W. Froncisz, J. S. Hyde, J. R. Pilbrow, and G. R. Sinclair. 1985. Direct evidence of nitrogen coupling in copper(II) complex of bovine serum albumin by S-band electron spin resonance technique. J. Inorg. Biochem. 25:217-224.
20. Rosenzweig, A. C., C. A. Frederick, S. J. Lippard, and P. Nordlund. 1993. Crystal structure of a bacterial non-human iron hydroxylase that catalyses the biological oxidation of methane. Nature. 366:537-543.
21. Semrau, J. D., A. Chistoserdov, J. Lebron, A. Costello, J. Davagnino, E. Kenna, A. J. Holmes, R. Finch, J. C. Murrell, and M. E. Lidstrom. 1995. Particulate methane monooxygenase genes in methanotrophs. J. Bacteriol 177:3071-3079.
22. cat by copper (II). J. Inorg. Biochem. 17:109-120.
23. Whittenbury, R., K. C. Phillips, and J. F. Wilkinson. 1970. Enrichment, isolation, and some properties of methane-utilizing bacteria. J. Gen. Microbiol. 61:205-218.
24. Yuan, H., M. L. P. Collins, and W. E. Antholine. 1997. Low frequency EPR of the copper in particulate methane monooxygenase from Methylomicrobium album BG8. J. Am. Chem. Soc. 119:5073-5074.
25. Yuan, H., M. L. P. Collins, and W. E. Antholine. 1998. Analysis of type 2 Cu(2+) in pMMO from M. album BG8. Biophys. J. 74:A300.
26. Yuan, H., M. L. P. Collins, and W. E. Antholine. 1999. Concentration of Cu, EPR-detectable Cu, and formation of cupric-ferrocyanide in membranes with pMMO. J. Inorg. Biochem. In press.
27. Zahn, J. A., and A. A. DiSpirito. 1996. Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J. Bacteriol. 178:1018-1029.