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PURIFICATION AND CHARACTERIZATION OF THE SOLUBLE METHANE MONOOXYGENASE FROM METHYLOSINUS-SPORIUM-5 DEMONSTRATES THE HIGHLY CONSERVED NATURE OF THIS ENZYME IN METHANOTROPHS
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UNSPECIFIED. (1991) PURIFICATION AND CHARACTERIZATION OF THE SOLUBLE METHANE MONOOXYGENASE FROM METHYLOSINUS-SPORIUM-5 DEMONSTRATES THE HIGHLY CONSERVED NATURE OF THIS ENZYME IN METHANOTROPHS. FEMS MICROBIOLOGY LETTERS, 78 (1). pp. 103-108. ISSN 0378-1097
Full text not available from this repository.Abstract
The type II obligate methanotroph Methylosinus sporium 5 was shown to have the ability to produce either a soluble or particulate methane monooxygenase dependent on the cooper to biomass ratio during growth. Two proteins of the soluble methane monooxygenase enzyme, proteins A (the hydroxylase) and C (the NADH-acceptor reductase) were purified and characterised, and shown to be very similar to those previously described in other organisms. Evidence is also presented for the existence of the third protein, protein B, in this enzyme complex.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QR Microbiology |
| Journal or Publication Title: | FEMS MICROBIOLOGY LETTERS |
| Publisher: | ELSEVIER SCIENCE BV |
| ISSN: | 0378-1097 |
| Date: | February 1991 |
| Volume: | 78 |
| Number: | 1 |
| Number of Pages: | 6 |
| Page Range: | pp. 103-108 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/22818 |
Data sourced from Thomson Reuters' Web of Knowledge
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