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PDBsum entry 3c8y
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Oxidoreductase
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PDB id
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3c8y
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References listed in PDB file
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Key reference
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Title
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Dithiomethylether as a ligand in the hydrogenase h-Cluster.
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Authors
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A.S.Pandey,
T.V.Harris,
L.J.Giles,
J.W.Peters,
R.K.Szilagyi.
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Ref.
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J Am Chem Soc, 2008,
130,
4533-4540.
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PubMed id
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Abstract
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An X-ray crystallographic refinement of the H-cluster of [FeFe]-hydrogenase from
Clostridium pasteurianum has been carried out to close-to atomic resolution and
is the highest resolution [FeFe]-hydrogenase presented to date. The 1.39 A,
anisotropically refined [FeFe]-hydrogenase structure provides a basis for
examining the outstanding issue of the composition of the unique nonprotein
dithiolate ligand of the H-cluster. In addition to influencing the electronic
structure of the H-cluster, the composition of the ligand has mechanistic
implications due to the potential of the bridge-head gamma-group participating
in proton transfer during catalysis. In this work, sequential density functional
theory optimizations of the dithiolate ligand embedded in a 3.5-3.9 A protein
environment provide an unbiased approach to examining the most likely
composition of the ligand. Structural, conformational, and energetic
considerations indicate a preference for dithiomethylether as an H-cluster
ligand and strongly disfavor the dithiomethylammonium as a catalytic base for
hydrogen production.
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