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Journal of Bacteriology, December 1998, p. 6440-6445, Vol. 180, No. 24
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cytochrome P460 Genes from the Methanotroph Methylococcus capsulatus Bathdagger

David J. Bergmann,1 James A. Zahn,1,Dagger Alan B. Hooper,2 and Alan A. DiSpirito1,*

Department of Microbiology, Iowa State University, Ames, Iowa 50011,1 and Department of Genetics and Cell Biology, University of Minnesota, St. Paul, Minnesota 551082

Received 20 May 1998/Accepted 28 September 1998

P460 cytochromes catalyze the oxidation of hydroxylamine to nitrite. They have been isolated from the ammonia-oxidizing bacterium Nitrosomonas europaea (R. H. Erickson and A. B. Hooper, Biochim. Biophys. Acta 275:231-244, 1972) and the methane-oxidizing bacterium Methylococcus capsulatus Bath (J. A. Zahn et al., J. Bacteriol. 176:5879-5887, 1994). A degenerate oligonucleotide probe was synthesized based on the N-terminal amino acid sequence of cytochrome P460 and used to identify a DNA fragment from M. capsulatus Bath that contains cyp, the gene encoding cytochrome P460. cyp is part of a gene cluster that contains three open reading frames (ORFs), the first predicted to encode a 59,000-Da membrane-bound polypeptide, the second predicted to encode a 12,000-Da periplasmic protein, and the third (cyp) encoding cytochrome P460. The products of the first two ORFs have no apparent similarity to any proteins in the GenBank database. The overall sequence similarity of the P460 cytochromes from M. capsulatus Bath and N. europaea was low (24.3% of residues identical), although short regions of conserved residues are present in the two proteins. Both cytochromes have a C-terminal, c-heme binding motif (CXXCH) and a conserved lysine residue (K61) that may provide an additional covalent cross-link to the heme (D. M. Arciero and A. B. Hooper, FEBS Lett. 410:457-460, 1997). Gene probing using cyp indicated that a cytochrome P460 similar to that from M. capsulatus Bath may be present in the type II methanotrophs Methylosinus trichosporium OB3b and Methylocystis parvus OBBP but not in the type I methanotrophs Methylobacter marinus A45, Methylomicrobium albus BG8, and Methylomonas sp. strains MN and MM2. Immunoblot analysis with antibodies against cytochrome P460 from M. capsulatus Bath indicated that the expression level of cytochrome P460 was not affected either by expression of the two different methane monooxygenases or by addition of ammonia to the culture medium.

* Corresponding author. Mailing address: Department of Microbiology, Iowa State University, 207 Science Building I, Ames, IA 50011-3211. Phone: (515) 294-2944. Fax: (515) 294-6019. E-mail: aland{at}iastate.edu.

dagger Journal paper J-18098 from the Agriculture and Home Economics Experiment Station, Ames, Iowa (project 3252).

Dagger Present address: Natural Products Research and Development, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285. 

Journal of Bacteriology, December 1998, p. 6440-6445, Vol. 180, No. 24
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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