Version 1
: Received: 5 January 2017 / Approved: 5 January 2017 / Online: 5 January 2017 (18:09:32 CET)
Version 2
: Received: 7 January 2017 / Approved: 9 January 2017 / Online: 9 January 2017 (02:49:00 CET)
How to cite:
Petrenko, A.; Stein, M. Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer. Preprints2017, 2017010029. https://doi.org/10.20944/preprints201701.0029.v1
Petrenko, A.; Stein, M. Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer. Preprints 2017, 2017010029. https://doi.org/10.20944/preprints201701.0029.v1
Petrenko, A.; Stein, M. Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer. Preprints2017, 2017010029. https://doi.org/10.20944/preprints201701.0029.v1
APA Style
Petrenko, A., & Stein, M. (2017). Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer. Preprints. https://doi.org/10.20944/preprints201701.0029.v1
Chicago/Turabian Style
Petrenko, A. and Matthias Stein. 2017 "Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer" Preprints. https://doi.org/10.20944/preprints201701.0029.v1
Abstract
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.
Keywords
electron transfer; Marcus equation; enzymatic fuel cell; hydrogen oxidation; electrode adsorption; DFT; bioelectrochemistry
Subject
Chemistry and Materials Science, Theoretical Chemistry
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.