The Modular Assembly of Clusters Is the Natural Synthetic Strategy for the Active Site of [FeFe] Hydrogenase | Zendy

Bethel Ryan D. | Zendy; Singleton Michael L. | Zendy; Darensbourg Marcetta Y. | Zendy

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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.

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