Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kenneth D. Karlin | - |
dc.date.accessioned | 2016-08-28T12:08:45Z | - |
dc.date.available | 2016-08-28T12:08:45Z | - |
dc.date.issued | 2010 | - |
dc.identifier.issn | 1433-7851 | - |
dc.identifier.other | OAK-6951 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/221083 | - |
dc.description.abstract | What/where is the active site? The determination of the metal ion content and makeup of the bacterial membrane protein methane monooxygenase (pMMO) has an enigmatic research history, despite protein X-ray structures. A new study appears to settle the issue; the dicopper center facilitates oxidation of methane to methanol. However, the unusual activesite environment leaves many questions for future investigations on the relevant copper-dioxygen chemistry and biochemistry. (Figure Presented) © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. | - |
dc.language | English | - |
dc.title | One is lonely and three is a crowd: Two coppers are for methane oxidation | - |
dc.type | Article | - |
dc.relation.issue | 38 | - |
dc.relation.volume | 49 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.startpage | 6714 | - |
dc.relation.lastpage | 6716 | - |
dc.relation.journaltitle | Angewandte Chemie - International Edition | - |
dc.identifier.doi | 10.1002/anie.201003403 | - |
dc.identifier.wosid | WOS:000282541300002 | - |
dc.identifier.scopusid | 2-s2.0-77956571266 | - |
dc.author.google | Himes R.A. | - |
dc.author.google | Barnese K. | - |
dc.author.google | Karlin K.D. | - |
dc.date.modifydate | 20160429000000 | - |