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Open AccessArticle

Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer

Max Planck Institute for Dynamics of Complex Technical Systems, Molecular Simulations and Design Group, Sandtorstrasse 1, 39106 Magdeburg, Germany
Author to whom correspondence should be addressed.
Academic Editor: Samuel De Visser
Int. J. Mol. Sci. 2017, 18(1), 100;
Received: 16 December 2016 / Revised: 28 December 2016 / Accepted: 30 December 2016 / Published: 5 January 2017
(This article belongs to the Special Issue Computational Modelling of Enzymatic Reaction Mechanisms)
Biohydrogen is a versatile energy carrier for the generation of electric energy from renewable sources. Hydrogenases can be used in enzymatic fuel cells to oxidize dihydrogen. The rate of electron transfer (ET) at the anodic side between the [NiFe]-hydrogenase enzyme distal iron–sulfur cluster and the electrode surface can be described by the Marcus equation. All parameters for the Marcus equation are accessible from Density Functional Theory (DFT) calculations. The distal cubane FeS-cluster has a three-cysteine and one-histidine coordination [Fe4S4](His)(Cys)3 first ligation sphere. The reorganization energy (inner- and outer-sphere) is almost unchanged upon a histidine-to-cysteine substitution. Differences in rates of electron transfer between the wild-type enzyme and an all-cysteine mutant can be rationalized by a diminished electronic coupling between the donor and acceptor molecules in the [Fe4S4](Cys)4 case. The fast and efficient electron transfer from the distal iron–sulfur cluster is realized by a fine-tuned protein environment, which facilitates the flow of electrons. This study enables the design and control of electron transfer rates and pathways by protein engineering. View Full-Text
Keywords: electron transfer; Marcus equation; enzymatic fuel cell; hydrogen oxidation; electrode adsorption; DFT; bioelectrochemistry electron transfer; Marcus equation; enzymatic fuel cell; hydrogen oxidation; electrode adsorption; DFT; bioelectrochemistry
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MDPI and ACS Style

Petrenko, A.; Stein, M. Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer. Int. J. Mol. Sci. 2017, 18, 100.

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