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rdf:type |
|
|
lifeskim:mentions |
|
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pubmed:issue |
6
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|
pubmed:dateCreated |
2003-5-27
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pubmed:abstractText |
The reaction catalyzed by the light-driven enzyme protochlorophyllide oxidoreductase (POR) has been initiated with a 50-fs laser pulse. We show that the catalytic mechanism, involving proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. It is known that catalysis by POR involves thermally excited protein dynamics; our results show that these molecular motions occur on an ultrafast timescale.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1072-8368
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
10
|
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
491-2
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
|
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pubmed:year |
2003
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pubmed:articleTitle |
Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase.
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|
pubmed:affiliation |
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK.
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|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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