Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 98, Issue 5, Pages 862-877Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2004.03.002
Keywords
[NiFe] hydrogenase; density functional theory; enzymatic mechanism; electron paramagnetic resonance; hydrogen metabolism
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Structures and spectroscopic observables of the paramagnetic intermediates of the enzymatic reaction cycle of the metalloenzyme [NiFe] hydrogenase were calculated using relativistic density functional theory (DFT) within the zero-order regular approximation (ZORA). By comparing experimental and calculated magnetic resonance parameters (g- and hyperfine tensors) for the states Ni-A, Ni-B, Ni-C, Ni-L, and Ni-CO the details of the atomic composition of these paramagnetic intermediates could be elucidated that are mostly not available from X-ray structure analysis. In general, good agreement between calculated and experimental observables could be obtained. A detailed picture of the changes of the active center during the catalytic cycle was deduced from the obtained structures. Based on these results, a consistent model for the sequence of redox states including protonation steps is proposed which is important for understanding the mechanism of the [NiFe] hydrogenase. (C) 2004 Elsevier Inc. All rights reserved.
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