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| [[Image:1feh.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1feh| PDB=1feh | SCENE= }} | | {{STRUCTURE_1feh| PDB=1feh | SCENE= }} |
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| '''FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM'''
| | ===FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9836629}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9836629 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9836629}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Seefeldt, L C.]] | | [[Category: Seefeldt, L C.]] |
| [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:13:53 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:07:34 2008'' |
