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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.

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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
Official Date: February 1991
Dates:
DateEvent
February 1991UNSPECIFIED
Volume: 78
Number: 1
Number of Pages: 6
Page Range: pp. 103-108
Publication Status: Published

Data sourced from Thomson Reuters' Web of Knowledge

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