Open AccessPurification and characterisation of the soluble methane monooxygenase from Methylosinus sporium 5 demonstrates the highly conserved nature of this enzyme in methanotrophs
Author(s) -
Pilkington S.J.,
Dalton H.
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04426.x
Subject(s) - methane monooxygenase , methanotroph , biochemistry , monooxygenase , enzyme , chemistry , reductase , anaerobic oxidation of methane , catalysis , cytochrome p450
Summary 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 copper 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.