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

Ryan D. Bethel, Michael L. Singleton, Marcetta Y. Darensbourg

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)8567-8569
Number of pages3
JournalAngewandte Chemie - International Edition
Volume49
Issue number46
DOIs
StatePublished - Nov 8 2010

Funding

Keywords

  • active sites
  • biosynthesis
  • hydrogenases
  • ironsulfur clusters

ASJC Scopus subject areas

  • General Chemistry
  • Catalysis

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