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 Å 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.
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Volbeda, A., Charon, MH., Piras, C. et al. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas. Nature 373, 580–587 (1995). https://doi.org/10.1038/373580a0
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DOI: https://doi.org/10.1038/373580a0
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