Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
- 1 February 1995
- journal article
- Published by Springer Nature in Nature
- Vol. 373 (6515), 580-587
- https://doi.org/10.1038/373580a0
Abstract
The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 A resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways.Keywords
This publication has 42 references indexed in Scilit:
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Influence of illumination on the electronic interaction between 77Se and nickel in active F420‐non‐reducing hydrogenase from Methanococcus voltaeFEBS Letters, 1993
- Carboxy‐terminal processing of the large subunit of [NiFe] hydrogenasesFEBS Letters, 1993
- Nickel and iron-sulphur centres in Desulfovibrio gigas hydrogenase: ESR spectra, redox properties and interactionsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- EPR evidence for direct interaction of carbon monoxide with nickel in hydrogenase from Chromatium vinosumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Monovalent nickel in hydrogenase from Chromatium vinosumFEBS Letters, 1985
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- HydrogenaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1980
- Characterization of the periplasmic hydrogenase from Desulfovibrio gigasBiochemical and Biophysical Research Communications, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977