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dc.contributor.authorWang, Weixue
dc.contributor.authorIacob, Roxana E.
dc.contributor.authorLuoh, Rebecca P.
dc.contributor.authorEngen, John R.
dc.contributor.authorLippard, Stephen J.
dc.date.accessioned2015-06-22T14:10:58Z
dc.date.available2015-06-22T14:10:58Z
dc.date.issued2014-06
dc.date.submitted2014-05
dc.identifier.issn0002-7863
dc.identifier.issn1520-5126
dc.identifier.urihttp://hdl.handle.net/1721.1/97492
dc.description.abstractThe hydroxylation or epoxidation of hydrocarbons by bacterial multicomponent monooxygenases (BMMs) requires the interplay of three or four protein components. How component protein interactions control catalysis, however, is not well understood. In particular, the binding sites of the reductase components on the surface of their cognate hydroxylases and the role(s) that the regulatory proteins play during intermolecular electron transfer leading to the hydroxylase reduction have been enigmatic. Here we determine the reductase binding site on the hydroxylase of a BMM enzyme, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). We present evidence that the ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (Grant GM032134)en_US
dc.description.sponsorshipWaters Corporationen_US
dc.language.isoen_US
dc.publisherAmerican Chemical Society (ACS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/ja504688zen_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourceAmerican Chemical Societyen_US
dc.titleElectron Transfer Control in Soluble Methane Monooxygenaseen_US
dc.typeArticleen_US
dc.identifier.citationWang, Weixue, Roxana E. Iacob, Rebecca P. Luoh, John R. Engen, and Stephen J. Lippard. “Electron Transfer Control in Soluble Methane Monooxygenase.” Journal of the American Chemical Society 136, no. 27 (July 9, 2014): 9754–62. © 2014 American Chemical Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.mitauthorWang, Weixueen_US
dc.contributor.mitauthorLuoh, Rebecca P.en_US
dc.contributor.mitauthorLippard, Stephen J.en_US
dc.relation.journalJournal of the American Chemical Societyen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsWang, Weixue; Iacob, Roxana E.; Luoh, Rebecca P.; Engen, John R.; Lippard, Stephen J.en_US
dc.identifier.orcidhttps://orcid.org/0000-0002-2693-4982
mit.licensePUBLISHER_POLICYen_US


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