Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

Nature. 1995 Feb 16;373(6515):580-7. doi: 10.1038/373580a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Computer Graphics
  • Crystallography, X-Ray
  • Desulfovibrio / enzymology*
  • Electron Transport
  • Hydrogenase / chemistry*
  • Hydrogenase / metabolism
  • Iron / chemistry*
  • Iron-Sulfur Proteins / chemistry
  • Molecular Sequence Data
  • Nickel / chemistry*
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Protons


  • Iron-Sulfur Proteins
  • Protons
  • Nickel
  • Iron
  • nickel-iron hydrogenase
  • Hydrogenase