Abstract
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.
Keywords
CrystallographyChemistryHydrogenaseCubaneOxidoreductaseCluster (spacecraft)FerredoxinCrystal structureIron–sulfur clusterMoleculeActive siteHydrogenCatalysisEnzyme
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Publication Info
- Year
- 1998
- Type
- article
- Volume
- 282
- Issue
- 5395
- Pages
- 1853-1858
- Citations
- 1848
- Access
- Closed
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Cite This
John W. Peters
(1998).
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution.
, 282
(5395)
, 1853-1858.
https://doi.org/10.1126/science.282.5395.1853
Identifiers
- DOI
- 10.1126/science.282.5395.1853