ArticleThe journal of physical chemistry. B2013
Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: compensating changes in the electronic coupling and reorganization energies.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 25 citations in OpenAlex.
- Modulating Radical Propagation in Proteins by Proton-Coupled Electron Transfer and Hydrogen Bonding.Biochemistry · 2026Article
- Modulating radical propagation in proteins by proton-coupled electron transfer and hydrogen bonding.bioRxiv : the preprint server for biology · 2026Article
- Sources of non-Arrhenius electron transport in bacterial nanowires.Physical chemistry chemical physics : PCCP · 2026Article
- Sortase-mediated ligation of cytochrome c peroxidase and cytochrome c highlights the roles of dynamics and conformational specificity for interprotein electron transfer.Journal of inorganic biochemistry · 2026Article
- Nrf1 acts as a highly-conserved determinon for maintaining robust redox homeostasis in the eco-evo-devo process of life histories.Cell stress · 2025Review
- Why Do Most Aromatics Fail to Support Hole Hopping in the CytochromeThe journal of physical chemistry. B · 2021Article
- Oxalate decarboxylase uses electron hole hopping for catalysis.The Journal of biological chemistry · 2021Article
- Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping.Journal of the American Chemical Society · 2019Article
- Why Are DNA and Protein Electron Transfer So Different?Annual review of physical chemistry · 2019Review
- Hole Hopping Across a Protein-Protein Interface.The journal of physical chemistry. B · 2019Article
- Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase.Angewandte Chemie (International ed. in English) · 2017Article
- Constraints on the Radical Cation Center of Cytochrome c Peroxidase for Electron Transfer from Cytochrome c.Biochemistry · 2016Article
- Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.Journal of the American Chemical Society · 2016Article
- Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Electron Transfer Proteins as Electronic Conductors: Significance of the Metal and Its Binding Site in the Blue Cu Protein, Azurin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2015Article
- Could tyrosine and tryptophan serve multiple roles in biological redox processes?Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2015Article
- Charge transfer in dynamical biosystems, or the treachery of (static) images.Accounts of chemical research · 2015Review
- Tyrosine oxidation in heme oxygenase: examination of long-range proton-coupled electron transfer.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Charge recombination rate constants vary no more than 3-fold for interprotein ET in the Zn-substituted wild type (WT) cytochrome c peroxidase (CcP):cytochrome c (Cc) complex and in complexes with four mutants of the Cc protein (i.e., F82S, F82W, F82Y, and F82I), despite large differences in the ET distance. Theoretical analysis indicates that charge recombination for all complexes involves a combination of tunneling and hopping via Trp191. For three of the five structures (WT and F82S(W)), the protein favors hopping more than that in the other two structures that have longer heme → ZnP distances (F82Y(I)). Experimentally observed biexponential ET kinetics is explained by the complex locking in alternative coupling pathways, where the acceptor hole state is either primarily localized on ZnP (slow phase) or on Trp191 (fast phase). The large conformational differences between the CcP:Cc interface for the F82Y(I) mutants compared to that the WT and F82S(W) complexes are predicted to change the reorganization energies for the CcP:Cc ET reactions because of changes in solvent exposure and interprotein ET distances. Since the recombination reaction is likely to occur in the inverted Marcus regime, an increased reorganization energy compensates the decreased role for hopping recombination (and the longer transfer distance) in the F82Y(I) mutants. Taken together, coupling pathway and reorganization energy effects for the five protein complexes explain the observed insensitivity of recombination kinetics to donor-acceptor distance and docking pose and also reveals how hopping through aromatic residues can accelerate long-range ET.
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