The modular assembly of clusters is the natural synthetic strategy for the active site of [FeFe] hydrogenase. Academic Article

abstract

• The 6Fe supercluster that comprises the [FeFe] hydrogenase active site has been shown to involve a modular buildup of ironsulfur clusters. Only three accessory proteins are needed to produce the CN, CO, and -SCH 2NHCH2S- 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. 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

authors

• Darensbourg, Marcetta

published proceedings

• Angew Chem Int Ed Engl

author list (cited authors)

• Bethel, R. D., Singleton, M. L., & Darensbourg, M. Y.

citation count

• 17

complete list of authors

• Bethel, Ryan D||Singleton, Michael L||Darensbourg, Marcetta Y

publication date

• November 2010

publisher

• Wiley  Publisher

published in

• Angewandte Chemie International Edition  Journal

keywords

• Catalytic Domain
• Chlamydomonas Reinhardtii
• Hydrogenase
• Iron
• Iron-sulfur Proteins
• Protein Structure, Tertiary
• Sulfur

PubMed Central ID

• 20845347

Digital Object Identifier (DOI)

• 10.1002/anie.201003747

start page

• 8567

end page

• 8569

volume

• 49

issue

• 46

URL

• http%3A%2F%2Fdx.doi.org%2F10.1002%2Fanie.201003747