1feh
FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM
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OverviewOverview
A three-dimensional structure for the monomeric iron-containing, hydrogenase (CpI) from Clostridium pasteurianum was determined to 1.8, angstrom resolution by x-ray crystallography using multiwavelength, anomalous dispersion (MAD) phasing. CpI, an enzyme that catalyzes the, two-electron reduction of two protons to yield dihydrogen, was found to, contain 20 gram atoms of iron per mole of protein, arranged into five, distinct [Fe-S] clusters. The probable active-site cluster, previously, termed the H-cluster, was found to be an unexpected arrangement of six, iron atoms existing as a [4Fe-4S] cubane subcluster covalently bridged by, a cysteinate thiol to a [2Fe] subcluster. The iron atoms of the [2Fe], subcluster both exist with an octahedral coordination geometry and are, bridged to each other by three non-protein atoms, assigned as two sulfide, atoms and one carbonyl or cyanide molecule. This structure provides, insights into the mechanism of biological hydrogen activation and has, broader implications for [Fe-S] cluster structure and function in, biological systems.
About this StructureAbout this Structure
1FEH is a Single protein structure of sequence from Clostridium pasteurianum with HC1, SF4 and FES as ligands. Active as Ferredoxin hydrogenase, with EC number 1.12.7.2 Full crystallographic information is available from OCA.
ReferenceReference
X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution., Peters JW, Lanzilotta WN, Lemon BJ, Seefeldt LC, Science. 1998 Dec 4;282(5395):1853-8. PMID:9836629
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