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- Amanda S. Hakemian
- Departments of Biochemistry, Molecular Biology and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208;,
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- Amy C. Rosenzweig
- Departments of Biochemistry, Molecular Biology and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208;,
書誌事項
- 公開日
- 2007-06-07
- DOI
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- 10.1146/annurev.biochem.76.061505.175355
- 公開者
- Annual Reviews
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説明
<jats:p> Methanotrophic bacteria oxidize methane to methanol in the first step of their metabolic pathway. Two forms of methane monooxygenase (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. </jats:p>
収録刊行物
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- Annual Review of Biochemistry
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Annual Review of Biochemistry 76 (1), 223-241, 2007-06-07
Annual Reviews