title: Distal [FeS]-Cluster Coordination in [NiFe]-Hydrogenase Facilitates Intermolecular Electron Transfer.
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.
authors.affiliation: Max Planck Institute for Dynamics of Complex Technical Systems, Molecular Simulations and Design Group, Sandtorstrasse 1, 39106 Magdeburg, Germany. petrenko@mpi-magdeburg.mpg.de.
authors.forename: Alexander
authors.initials: A
authors.lastname: Petrenko
authors.affiliation: Max Planck Institute for Dynamics of Complex Technical Systems, Molecular Simulations and Design Group, Sandtorstrasse 1, 39106 Magdeburg, Germany. matthias.stein@mpi-magdeburg.mpg.de.
authors.forename: Matthias
authors.initials: M
authors.lastname: Stein
mesh_terms: D000465:Algorithms; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D003901:Desulfovibrio / Q000235:genetics / Q000378:metabolism; D004579:Electron Transport / Q000235:genetics; D004583:Electrons; D006639:Histidine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry* / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D009154:Mutation; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D006639:Histidine; D006859:Hydrogen; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D003545:Cysteine
keywords: DFT; Marcus equation; bioelectrochemistry; electrode adsorption; electron transfer; enzymatic fuel cell; hydrogen oxidation