Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph

Brian G. Fox, John D. Lipscomb

Research output: Contribution to journalArticle

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Abstract

The purification of the hydroxylase component of a 3 component methane monooxygenase from the type II methanotroph Methylosinus trichosporium OB3b is reported. The enzyme (240 kDa) has an (αβγ)2 subunit structure as observed for hydroxylases isolated from other Type I and Type II methanotrophs, but it exhibits a 5 to 10 fold higher specific activity and is isolated in 2 to 10 fold higher yield. EPR and Mössbauer spectra of the hydroxylase show that it contains a coupled iron center containing an even number of iron atoms. The spectra are similar to those of proteins known to contain oxo-bridged binuclear iron centers. The presence of such a center is unprecedented in a monooxygenase and suggests that a novel mechanism is utilized.

Original languageEnglish (US)
Pages (from-to)165-170
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume154
Issue number1
DOIs
StatePublished - Jul 15 1988

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