The biochemistry of methane oxidation

Amanda S. Hakemian, Amy C. Rosenzweig

Research output: Chapter in Book/Report/Conference proceedingChapter

252 Scopus citations

Abstract

Methanotrophic bacteria oxidize methane to methanol in the first step of their metabolic pathway. Two forms of methane monooxyge- nase (MMO) enzymes catalyze this reaction: soluble MMO (sMMO) and membrane-bound or particulate MMO (pMMO). pMMO is expressed when copper is available, and its active site is believed to contain copper. Whereas sMMO is well characterized, most aspects of pMMO biochemistry remain unknown and somewhat controversial. This review emphasizes advances in the past two to three years related to pMMO and to copper uptake and copper-dependent regulation in methanotrophs. The pMMO metal centers have been characterized spectroscopically, and the first pMMO crystal structure has been determined. Significant effort has been devoted to improving in vitro pMMO activity. Proteins involved in sMMO regulation and additional copper-regulated proteins have been identified, and the Methylococcus capsulatus (Bath) genome has been sequenced. Finally, methanobactin (mb), a small copper chelator proposed to facilitate copper uptake, has been characterized.

Original languageEnglish (US)
Title of host publicationAnnual Review of Biochemistry
Pages223-241
Number of pages19
DOIs
StatePublished - 2007

Publication series

NameAnnual Review of Biochemistry
Volume76
ISSN (Print)0066-4154
ISSN (Electronic)0066-4154

Keywords

  • Copper switch
  • Methanobactin
  • Methanotroph
  • Particulate methane monooxygenase

ASJC Scopus subject areas

  • Biochemistry

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