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Issue 43, 2014
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Modulation of active site electronic structure by the protein matrix to control [NiFe] hydrogenase reactivity

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Abstract

Control of the reactivity of the nickel center of the [NiFe] hydrogenase and other metalloproteins commonly involves outer coordination sphere ligands that act to modify the geometry and physical properties of the active site metal centers. We carried out a combined set of classical molecular dynamics and quantum/classical mechanics calculations to provide quantitative estimates of how dynamic fluctuations of the active site within the protein matrix modulate the electronic structure at the catalytic center. Specifically we focused on the dynamics of the inner and outer coordination spheres of the cysteinate-bound Ni–Fe cluster in the catalytically active Ni-C state. There are correlated movements of the cysteinate ligands and the surrounding hydrogen-bonding network, which modulate the electron affinity at the active site and the proton affinity of a terminal cysteinate. On the basis of these findings, we hypothesize a coupling between protein dynamics and electron and proton transfer reactions critical to dihydrogen production.

Graphical abstract: Modulation of active site electronic structure by the protein matrix to control [NiFe] hydrogenase reactivity

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Article information


Submitted
06 Aug 2014
Accepted
30 Sep 2014
First published
30 Sep 2014

Phys. Chem. Chem. Phys., 2014,16, 24026-24033
Article type
Paper

Modulation of active site electronic structure by the protein matrix to control [NiFe] hydrogenase reactivity

D. M. A. Smith, S. Raugei and T. C. Squier, Phys. Chem. Chem. Phys., 2014, 16, 24026
DOI: 10.1039/C4CP03518F

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