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The Modular Assembly of Clusters Is the Natural Synthetic Strategy for the Active Site of [FeFe] Hydrogenase
Author(s) -
Bethel Ryan D.,
Singleton Michael L.,
Darensbourg Marcetta Y.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201003747
Subject(s) - active site , hydrogenase , chemistry , modular design , scaffold protein , biochemistry , enzyme , computer science , signal transduction , operating system
The 6Fe supercluster that comprises the [FeFe] hydrogenase active site has been shown to involve a modular buildup of iron–sulfur clusters. Only three accessory proteins are needed to produce the CN − , CO, and μ‐SCH 2 NHCH 2 S‐ units that bind to the 2Fe2S subcluster precursor. The scaffold/carrier protein inserts the preformed 2Fe subcluster into the apoprotein through a channel, which then closes to encapsulate the completed active site.