Application of the Marcus equation to methyl transfers

1986 ◽  
Vol 90 (16) ◽  
pp. 3756-3759 ◽  
Author(s):  
Edward S. Lewis
Keyword(s):  
Marcus Equation

An extension of the Marcus equation: the Marcus potential energy function

2018 ◽  
Vol 24 (4) ◽  
Author(s):  
Soledad Gutiérrez-Oliva ◽  
Bárbara Herrera ◽  
Alejandro Toro-Labbé
Keyword(s):  
Potential Energy ◽  
Energy Function ◽  
Potential Energy Function ◽  
Marcus Equation

Energy and chemical force profiles from the Marcus equation

2004 ◽  
Vol 392 (1-3) ◽  
pp. 132-139 ◽  
Author(s):  
Jorge Martı́nez ◽  
Alejandro Toro-Labbé
Keyword(s):  
Marcus Equation ◽  
Force Profiles ◽  
Chemical Force

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

2017 ◽  
Author(s):  
Alexander Petrenko ◽  
Matthias Stein
Keyword(s):  
Electron Transfer ◽  
Density Functional ◽  
Electric Energy ◽  
Reorganization Energy ◽  
Outer Sphere ◽  
Intermolecular Electron Transfer ◽  
Sulfur Cluster ◽  
Donor And Acceptor ◽  
Marcus Equation ◽  
Hydrogenase Enzyme

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.

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