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Methane oxidation by the copper methane monooxygenase: Before and after the cryogenic electron microscopy structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath)

Chan, Sunney I. and Wang, Vincent C.-C. and Chen, Peter P.-Y. and Yu, Steve S.-F. (2022) Methane oxidation by the copper methane monooxygenase: Before and after the cryogenic electron microscopy structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath). Journal of the Chinese Chemical Society . ISSN 0009-4536. doi:10.1002/jccs.202200166. (In Press) https://resolver.caltech.edu/CaltechAUTHORS:20220708-259535200

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Abstract

The particulate methane monooxygenase (pMMO) is a copper monooxygenase that converts methane into methanol in methanotrophic bacteria. As this enzyme converts methane into methanol efficiently and selectively under ambient conditions, it has become the paradigm for understanding the design of nature to facilitate this process so that we could develop a biomimetic catalyst to accomplish this difficult C1 chemistry in the laboratory. With the advent of the recent 2.5 Å cryo-electron microscopy structure of the pMMO from Methylococcus capsulatus (Bath), it is now evident that the catalytic site of hydroxylation in pMMO is a Cu^ICu^ICu^I tricopper cluster (Cu^I: copper ions) sequestered within the transmembrane domain of this protein complex. With three reducing equivalents embodied in this structural motif, the tricopper cluster can react with O₂ to irreversibly cleave the O-O bond to harness the highly reactive oxene for rapid and direct insertion into the C-H bonds of methane. Here, we review the structural, biochemical, and biophysical studies over the past three decades that have culminated in this important advance in the chemistry of methane oxidation.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1002/jccs.202200166DOIArticle
ORCID:
AuthorORCID
Chan, Sunney I.0000-0002-5348-2723
Additional Information:© 2022 Chemical Society Located in Taipei and Wiley-VCH GmbH. Version of Record online: 23 May 2022; Manuscript accepted: 08 May 2022; Manuscript received: 13 April 2022. Dedicated to the memory of Robert H. Grubbs, a great scientist and human being. Funding information: Ministry of Science and Technology, Taiwan, Grant/Award Numbers: 110-2113-M-001-038, 109-2113-M-001-003; Academia Sinica, Grant/Award Numbers: AS-KPQ-106-DDPP, AS-TP-108-ML07, AS-GCS-107-07
Funders:
Funding AgencyGrant Number
Ministry of Science and Technology (Taipei)110-2113-M-001-038
Ministry of Science and Technology (Taipei)109-2113-M-001-003
Academia SinicaAS-KPQ-106-DDPP
Academia SinicaAS-TP-108-ML07
Academia SinicaAS-GCS-107-07
Subject Keywords:biocatalysis; copper monooxygenase; methane oxidation; oxene chemistry; tricopper cluster
DOI:10.1002/jccs.202200166
Record Number:CaltechAUTHORS:20220708-259535200
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20220708-259535200
Official Citation:Methane oxidation by the copper methane monooxygenase: Before and after the cryogenic electron microscopy structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath). Chan, S. I., Wang, V. C., Chen, P. P.-Y., Yu, S. S.-F., J. Chin. Chem. Soc. 2022, 1. https://doi.org/10.1002/jccs.202200166
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:115443
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:11 Jul 2022 17:57
Last Modified:11 Jul 2022 17:57

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