| Literature DB >> 16137685 |
Jon K Rubach1, Xavier Brazzolotto, Jacques Gaillard, Marc Fontecave.
Abstract
Fe-only hydrogenases contain a di-iron active site complex, in which the two Fe atoms have carbon monoxide and cyanide ligands and are linked together by a putative di(thiomethyl)amine molecule. We have cloned, purified and characterized the HydE and HydG proteins, thought to be involved in the biosynthesis of this peculiar metal site, from the thermophilic organism Thermotoga maritima. The HydE protein anaerobically reconstituted with iron and sulfide binds two [4Fe-4S] clusters, as characterized by UV and EPR spectroscopy. The HydG protein binds one [4Fe-4S] cluster, and probably an additional one. Both enzymes are able to reductively cleave S-adenosylmethionine (SAM) when reduced by dithionite, confirming that they are Radical-SAM enzymes.Entities:
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Year: 2005 PMID: 16137685 DOI: 10.1016/j.febslet.2005.07.092
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124