Journal
DALTON TRANSACTIONS
Volume -, Issue 21, Pages 4030-4038Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b304316a
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This Perspective describes, from our own personal experiences, how the architecture of the NiFe hydrogenase active site has been elucidated by a combination of protein crystallography, Electron paramagnetic resonance and Fourier transform infrared spectroscopic studies. Thus within a period of eight years our perception of the active center has changed from a mononuclear Ni center with S and N/O coordination to a binuclear NiFe unit with thiolate (to Ni and Fe) and CO and CN- (to Fe) ligands. This biologically unusual organometallic cluster poses a real challenge in terms of understanding the role of its different components. Current ideas concerning the NiFe hydrogenase catalytic mechanism are discussed in this context.
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