skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Thermodynamic Hydricity of [FeFe]-Hydrogenases

Abstract

In this Perspective, recent advances in the mechanistic understanding of [FeFe]-hydrogenases are analyzed using thermodynamic principles that have been instrumental for the rational design of state-of-the-art molecular electrocatalysts for production and oxidation of H2. After remaining elusive for many years, a terminal hydride state has now been identified in several native and artificial [FeFe]-hydrogenases. Determination of the hydricity of this crucial catalytic intermediate reveals that modification of amino acid residues in the proton transport channel changes the intrinsic thermodynamic bias of the enzyme to favor oxidation of H2 via heterolytic cleavage of the H H bond. From this vantage point, the structure and catalytic function of the hydride state and the controversial super-reduced state are considered with an eye towards key hydrogen bonding interactions between the active site and the extended protein environment. This research was supported as part of the Center for Molecular Electrocatalysis, an Energy Frontier Research Center funded by the U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences. Pacific Northwest National Laboratory is operated by Battelle for DOE.

Authors:
ORCiD logo [1]
  1. BATTELLE (PACIFIC NW LAB)
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1530850
Report Number(s):
PNNL-SA-140083
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 141; Journal Issue: 18
Country of Publication:
United States
Language:
English

Citation Formats

Wiedner, Eric S. Thermodynamic Hydricity of [FeFe]-Hydrogenases. United States: N. p., 2019. Web. doi:10.1021/jacs.8b13084.
Wiedner, Eric S. Thermodynamic Hydricity of [FeFe]-Hydrogenases. United States. doi:10.1021/jacs.8b13084.
Wiedner, Eric S. Wed . "Thermodynamic Hydricity of [FeFe]-Hydrogenases". United States. doi:10.1021/jacs.8b13084.
@article{osti_1530850,
title = {Thermodynamic Hydricity of [FeFe]-Hydrogenases},
author = {Wiedner, Eric S.},
abstractNote = {In this Perspective, recent advances in the mechanistic understanding of [FeFe]-hydrogenases are analyzed using thermodynamic principles that have been instrumental for the rational design of state-of-the-art molecular electrocatalysts for production and oxidation of H2. After remaining elusive for many years, a terminal hydride state has now been identified in several native and artificial [FeFe]-hydrogenases. Determination of the hydricity of this crucial catalytic intermediate reveals that modification of amino acid residues in the proton transport channel changes the intrinsic thermodynamic bias of the enzyme to favor oxidation of H2 via heterolytic cleavage of the H H bond. From this vantage point, the structure and catalytic function of the hydride state and the controversial super-reduced state are considered with an eye towards key hydrogen bonding interactions between the active site and the extended protein environment. This research was supported as part of the Center for Molecular Electrocatalysis, an Energy Frontier Research Center funded by the U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences. Pacific Northwest National Laboratory is operated by Battelle for DOE.},
doi = {10.1021/jacs.8b13084},
journal = {Journal of the American Chemical Society},
number = 18,
volume = 141,
place = {United States},
year = {2019},
month = {5}
}