1H2A

SINGLE CRYSTALS OF HYDROGENASE FROM DESULFOVIBRIO VULGARIS

Summary for 1H2A

• Entry DOI: 10.2210/pdb1h2a/pdb
• Descriptor: HYDROGENASE, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (7 entities in total)
• Functional Keywords: ni-fe hydrogenase, so ligand, hydrogen metabolism, mg center, mir, mad, oxidoreductase
• Biological source: Desulfovibrio vulgaris str. 'Miyazaki F'; More
• Cellular location: Periplasm: P21853 P21852
• Total number of polymer chains: 2
• Total formula weight: 98134.54

Authors

Higuchi, Y.,Yasuoka, N. (deposition date: 1997-10-17, release date: 1999-02-09, Last modification date: 2024-02-07)

Primary citation

Higuchi, Y.,Yagi, T.,Yasuoka, N.
Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis.
Structure, 5:1671-1680, 1997

PubMed Abstract: The hydrogenase of Desulfovibrio sp. catalyzes the reversible oxidoreduction of molecular hydrogen, in conjunction with a specific electron acceptor, cytochrome c3. The Ni-Fe active center of Desulfovibrio hydrogenase has an unusual ligand structure with non-protein ligands. An atomic model at high resolution is required to make concrete assignment of the ligands which coordinate the Ni-Fe center. These in turn will provide insight into the mechanism of electron transfer, during the reaction catalysed by hydrogenase.

PubMed: 9438867
DOI: 10.1016/S0969-2126(97)00313-4

Experimental method

X-RAY DIFFRACTION (1.8 Å)