Cited by 189Metal-Catalyzed Oxygenation MechanismsPhotochemistry and Electron Transfer StudiesChemical Reaction Mechanisms

Proton-coupled electron transfer: a unifying mechanism for biological charge transport, amino acid radical initiation and propagation, and bond making/breaking reactions of water and oxygen

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Chang, Christopher J., Chang, Michelle C.Y., Damrauer, Niels H., Nocera, Daniel G.·2004·Biochimica et Biophysica Acta (BBA) - Bioenergetics

Abstract

Redox-driven proton pumps, radical initiation and propagation in biology, and small-molecule activation processes all involve the coupling of electron transfer to proton transport. A mechanistic framework in which to interpret these processes is being developed by examining proton-coupled electron transfer (PCET) in model and natural systems. Specifically, PCET investigations are underway on the following three fronts: (1) the elucidation of the PCET reaction mechanism by time-resolved laser spectroscopy of electron donors and acceptors juxtaposed by a proton transfer interface; (2) the role of amino acid radicals in biological catalysis with the radical initiation and transport processes of E. coli ribonucleotide reductase (RNR) as a focal point; and (3) the application of PCET towards small-molecule activation with emphasis on biologically relevant bond-breaking and bond-making processes involving oxygen and water. A review of recent developments in each of these areas is discussed.

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Crossref · 10.1016/j.bbabio.2003.08.010

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  • Proton-coupled electron transfer mechanisms have been shown to underlie the activation of most substrate bonds at enzyme-active sites.

    “In biological energy storage, the importance of proton translocation driven by electron transfer was first noted in 1961 [89], and since then, proton-coupled electron transfer mechanisms [90] have been shown to underlie amino acid radical generation and transport [91] along with the activation of most substrate bonds at enzyme-active sites [92].”

    From The future of quantum biology (2018) · cites this paper as [92]

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Research works printed but not linked: 2

  1. M.C.Y. Chang, Ph.D. Thesis, MIT (2004).
  2. H.B. Dunford, Heme Peroxidases, Wiley, New York, 1999.

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Authors
Chang, C. J., Chang, M. C. Y., Damrauer, N. H., & Nocera, D. G.
Affiliations
Massachusetts Institute of Technology (US)
Corresponding author
Nocera, Daniel G.
Venue
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher
Elsevier BV
Published
2004-04
Volume
1655
Issue
1-3
Pages
13-28
ISSN
0005-2728 (ISSN-L)
OpenAlex
W2096239090
Cited by
189
References
117
Citations by year
2026: 2 · 2025: 5 · 2024: 4 · 2023: 4 · 2022: 6 · 2021: 9 · 2020: 3 · 2019: 6 · 2018: 7 · 2017: 7 · 2016: 9 · 2015: 9 · 2014: 7 · 2013: 1 · 2012: 11
FWCI
1.09
Type
journal article
Language
en
Open access
Locations
  • Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM47274, R01GM047274)
Topics
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
Keywords
proton-coupled electron transfer, amino acid radicals, radical initiation, radical propagation, ribonucleotide reductase, Escherichia coli, small molecule activation, oxygen activation, water activation, time-resolved laser spectroscopy, reaction mechanism
MeSH terms
Amino Acids, Electron Transport Complex IV, Electron Transport, Free Radicals, Models, Biological, Oxidation-Reduction, Oxygen, Photolysis, Ribonucleotide Reductases, Water, Proton-Motive Force, Photosystem II Protein Complex

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