1H2R

THREE-DIMENSIONAL STRUCTURE OF NI-FE HYDROGENASE FROM DESULFIVIBRIO VULGARIS MIYAZAKI F IN THE REDUCED FORM AT 1.4 A RESOLUTION

Summary for 1H2R

• Entry DOI: 10.2210/pdb1h2r/pdb
• Descriptor: PROTEIN (PERIPLASMIC [NIFE] HYDROGENASE SMALL SUBUNIT), PROTEIN (PERIPLASMIC [NIFE] HYDROGENASE LARGE SUBUNIT), IRON/SULFUR CLUSTER, ... (7 entities in total)
• Functional Keywords: high resolution crystal structure, sulfur-bridging ligand, ni-fe hydrogenase, reduced enzyme, atomic cap at active site, oxidoreductase
• Biological source: Desulfovibrio vulgaris str. 'Miyazaki F'; More
• Cellular location: Periplasm: P21853 P21852
• Total number of polymer chains: 2
• Total formula weight: 89244.11

Authors

Higuchi, Y.,Ogata, H. (deposition date: 1999-06-14, release date: 2000-01-05, Last modification date: 2023-08-09)

Primary citation

Higuchi, Y.,Ogata, H.,Miki, K.,Yasuoka, N.,Yagi, T.
Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 A resolution.
Structure Fold.Des., 7:549-556, 1999

PubMed Abstract: The active site of [NiFe] hydrogenase, a heterodimeric protein, is suggested to be a binuclear Ni-Fe complex having three diatomic ligands to the Fe atom and three bridging ligands between the Fe and Ni atoms in the oxidized form of the enzyme. Two of the bridging ligands are thiolate sidechains of cysteinyl residues of the large subunit, but the third bridging ligand was assigned as a non-protein monatomic sulfur species in Desulfovibrio vulgaris Miyazaki F hydrogenase.

PubMed: 10378274
DOI: 10.1016/S0969-2126(99)80071-9

Experimental method

X-RAY DIFFRACTION (1.4 Å)