Abstract
The first density functional calculations on high-spin (HS) Ni(II) models for the active site of the [NiFe] hydrogenases predict a ligand arrangement about Ni that is in better agreement with the crystal structures than previous predictions for low-spin (LS) Ni(II) models. With the crystal structures' geometry, the HS form is approximately 20 kcal/mol lower in energy than the LS one.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Binding Sites
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Desulfovibrio / enzymology
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Electron Spin Resonance Spectroscopy
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Hydrogenase / chemistry*
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Hydrogenase / metabolism
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Models, Molecular
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Nickel / chemistry*
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Organometallic Compounds / chemistry
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Protein Conformation
Substances
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Organometallic Compounds
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Nickel
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nickel-iron hydrogenase
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Hydrogenase