Literature DB >> 17444606

Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase.

Ramakrishnan Balasubramanian1, Amy C Rosenzweig.   

Abstract

Particulate methane monooxygense (pMMO) is an integral membrane copper-containing enzyme that converts methane to methanol. Knowledge of how pMMO selectively oxidizes methane under ambient conditions could impact the development of new catalysts. The crystal structure of Methylococcus capsulatus (Bath) pMMO reveals the composition and location of three metal centers. Spectroscopic data provide insight into the coordination environments and oxidation states of these metal centers. These results, combined with computational studies and comparisons to relevant systems, are discussed in the context of identifying the most likely site for O 2 activation.

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Year:  2007        PMID: 17444606     DOI: 10.1021/ar700004s

Source DB:  PubMed          Journal:  Acc Chem Res        ISSN: 0001-4842            Impact factor:   22.384


  43 in total

Review 1.  Structures of membrane proteins.

Authors:  Kutti R Vinothkumar; Richard Henderson
Journal:  Q Rev Biophys       Date:  2010-02       Impact factor: 5.318

Review 2.  Architecture and active site of particulate methane monooxygenase.

Authors:  Megen A Culpepper; Amy C Rosenzweig
Journal:  Crit Rev Biochem Mol Biol       Date:  2012-06-23       Impact factor: 8.250

3.  Perturbing the Copper(III)-Hydroxide Unit through Ligand Structural Variation.

Authors:  Debanjan Dhar; Gereon M Yee; Andrew D Spaeth; David W Boyce; Hongtu Zhang; Büsra Dereli; Christopher J Cramer; William B Tolman
Journal:  J Am Chem Soc       Date:  2015-12-22       Impact factor: 15.419

Review 4.  Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).

Authors:  Richard A Himes; Kenneth D Karlin
Journal:  Curr Opin Chem Biol       Date:  2009-03-13       Impact factor: 8.822

5.  Substrate and Lewis Acid Coordination Promote O-O Bond Cleavage of an Unreactive L2CuII2(O22-) Species to Form L2CuIII2(O)2 Cores with Enhanced Oxidative Reactivity.

Authors:  Isaac Garcia-Bosch; Ryan E Cowley; Daniel E Díaz; Ryan L Peterson; Edward I Solomon; Kenneth D Karlin
Journal:  J Am Chem Soc       Date:  2017-02-14       Impact factor: 15.419

6.  Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M.

Authors:  Stephen M Smith; Swati Rawat; Joshua Telser; Brian M Hoffman; Timothy L Stemmler; Amy C Rosenzweig
Journal:  Biochemistry       Date:  2011-11-03       Impact factor: 3.162

Review 7.  Structural biology of copper trafficking.

Authors:  Amie K Boal; Amy C Rosenzweig
Journal:  Chem Rev       Date:  2009-10       Impact factor: 60.622

Review 8.  Metals and Methanotrophy.

Authors:  Jeremy D Semrau; Alan A DiSpirito; Wenyu Gu; Sukhwan Yoon
Journal:  Appl Environ Microbiol       Date:  2018-03-01       Impact factor: 4.792

Review 9.  The tetranuclear copper active site of nitrous oxide reductase: the CuZ center.

Authors:  Simone Dell'Acqua; Sofia R Pauleta; Isabel Moura; José J G Moura
Journal:  J Biol Inorg Chem       Date:  2011-01-15       Impact factor: 3.358

10.  Copper(I)-alpha-ketocarboxylate complexes: characterization and O2 reactions that yield copper-oxygen intermediates capable of hydroxylating arenes.

Authors:  Sungjun Hong; Stefan M Huber; Laura Gagliardi; Christopher C Cramer; William B Tolman
Journal:  J Am Chem Soc       Date:  2007-10-25       Impact factor: 15.419

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