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Title: Hydrogen Tunneling in Enzymes and Biomimetic Models

Abstract

Hydrogen transfer reactions play an important role throughout chemistry and biology. In general, hydrogen transfer reactions encompass proton and hydride transfer, which are associated with the transfer of a positively or negatively charged species, respectively, and proton-coupled electron transfer (PCET), which corresponds to the net transfer of one electron and one proton in the simplest case. Such PCET reactions can occur by either a sequential mechanism, in which the proton or electron transfers first, or a concerted mechanism, in which the electron and proton transfer in a single kinetic step with no stable intermediate. Furthermore, concerted PCET reactions can be subdivided into hydrogen atom transfer (HAT), which corresponds to the transfer of an electron and proton between the same donor and acceptor (i.e., the transfer of a predominantly neutral species), and electron-proton transfer (EPT), which corresponds to the transfer of an electron and proton between different donors and acceptors, possibly even in different directions. In all of these types of hydrogen transfer reactions, hydrogen tunneling could potentially play a signficant role. The theoretical development portion of this Review was supported by the National Science Foundation under CHE-10-57875. The biological portion of this Review was funded by NIH Grant No. GM056207.more » The biomimetic portion was supported as part of the Center for Molecular Electro-catalysis, an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences.« less

Authors:
;
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1234800
Report Number(s):
PNNL-SA-105678
Journal ID: ISSN 0009-2665; KC0307010
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Journal Name:
Chemical Reviews
Additional Journal Information:
Journal Volume: 114; Journal Issue: 7; Journal ID: ISSN 0009-2665
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English

Citation Formats

Layfield, Joshua P., and Hammes-Schiffer, Sharon. Hydrogen Tunneling in Enzymes and Biomimetic Models. United States: N. p., 2013. Web. doi:10.1021/cr400400p.
Layfield, Joshua P., & Hammes-Schiffer, Sharon. Hydrogen Tunneling in Enzymes and Biomimetic Models. United States. doi:10.1021/cr400400p.
Layfield, Joshua P., and Hammes-Schiffer, Sharon. Fri . "Hydrogen Tunneling in Enzymes and Biomimetic Models". United States. doi:10.1021/cr400400p.
@article{osti_1234800,
title = {Hydrogen Tunneling in Enzymes and Biomimetic Models},
author = {Layfield, Joshua P. and Hammes-Schiffer, Sharon},
abstractNote = {Hydrogen transfer reactions play an important role throughout chemistry and biology. In general, hydrogen transfer reactions encompass proton and hydride transfer, which are associated with the transfer of a positively or negatively charged species, respectively, and proton-coupled electron transfer (PCET), which corresponds to the net transfer of one electron and one proton in the simplest case. Such PCET reactions can occur by either a sequential mechanism, in which the proton or electron transfers first, or a concerted mechanism, in which the electron and proton transfer in a single kinetic step with no stable intermediate. Furthermore, concerted PCET reactions can be subdivided into hydrogen atom transfer (HAT), which corresponds to the transfer of an electron and proton between the same donor and acceptor (i.e., the transfer of a predominantly neutral species), and electron-proton transfer (EPT), which corresponds to the transfer of an electron and proton between different donors and acceptors, possibly even in different directions. In all of these types of hydrogen transfer reactions, hydrogen tunneling could potentially play a signficant role. The theoretical development portion of this Review was supported by the National Science Foundation under CHE-10-57875. The biological portion of this Review was funded by NIH Grant No. GM056207. The biomimetic portion was supported as part of the Center for Molecular Electro-catalysis, an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences.},
doi = {10.1021/cr400400p},
journal = {Chemical Reviews},
issn = {0009-2665},
number = 7,
volume = 114,
place = {United States},
year = {2013},
month = {12}
}