Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

M.H. Sazinsky, M. Merkx, E. Cadieux, Sonya Tang, S.J. Lippard

Research output: Contribution to journalArticleAcademicpeer-review

30 Citations (Scopus)
1 Downloads (Pure)

Abstract

A three-component soluble methane monooxygenase (sMMO) enzyme system catalyzes the hydroxylation of methane to methanol at a carboxylate-bridged diiron center housed in the a-subunit of the hydroxylase (MMOH). Catalysis is facilitated by the presence of a regulatory protein (MMOB) and inhibited by MMOD, a protein of unknown function encoded in the sMMO operon. Both MMOB and MMOD are presumed to bind to the same region of the MMOH a-subunit. A colorimetric method for monitoring removal of Fe(II) from MMOH was developed using 1,10-phenanthroline and yields apo MMOH with
Original languageEnglish
Pages (from-to)16263-16276
JournalBiochemistry
Volume43
Issue number51
DOIs
Publication statusPublished - 2004

Fingerprint Dive into the research topics of 'Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)'. Together they form a unique fingerprint.

Cite this