1feh

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{{STRUCTURE_1feh| PDB=1feh | SCENE= }}
{{STRUCTURE_1feh| PDB=1feh | SCENE= }}
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'''FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM'''
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===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.
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{{ABSTRACT_PUBMED_9836629}}
==About this Structure==
==About this Structure==
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[[Category: Seefeldt, L C.]]
[[Category: Seefeldt, L C.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:07:34 2008''

Revision as of 00:07, 1 July 2008

Image:1feh.png

Template:STRUCTURE 1feh

FE-ONLY HYDROGENASE FROM CLOSTRIDIUM PASTEURIANUM

Template:ABSTRACT PUBMED 9836629

About this Structure

1FEH is a Single protein structure of sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA.

Reference

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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