Issue 21, 2005

The quest for the particulate methane monooxygenase active site

Abstract

Particulate methane monooxygenase is a copper-containing, membrane-bound metalloenzyme that converts methane to methanol in Nature. How pMMO accomplishes this difficult reaction under ambient conditions is one of the major unsolved problems in bioinorganic chemistry. Despite considerable research efforts in the past 20 years, the active site of the enzyme remains unknown. We recently solved the first crystal structure of pMMO to 2.8 Å resolution, revealing the overall structure, oligomerization state, subunit ratio, and composition and location of the metal centers. Almost none of the key structural features were predicted. In this Perspective, we review the state of knowledge before and after the structure determination, emphasizing elucidation of the pMMO active site.

Graphical abstract: The quest for the particulate methane monooxygenase active site

Article information

Article type
Perspective
Submitted
11 May 2005
Accepted
07 Jun 2005
First published
26 Sep 2005

Dalton Trans., 2005, 3390-3396

The quest for the particulate methane monooxygenase active site

R. L. Lieberman and A. C. Rosenzweig, Dalton Trans., 2005, 3390 DOI: 10.1039/B506651D

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