proton-coupled electron transfer

Kinetic model for reversible radical transfer in ribonucleotide reductase

328. R. Reinhardt, D. Konstantinovsky, A. V. Soudackov, and S. Hammes-Schiffer, “Kinetic model for reversible radical transfer in ribonucleotide reductase,” Proc. Nat. Acad. Sci. USA (in press).

Theoretical modeling of electrochemical proton-coupled electron transfer

323. R. E. Warburton, A. V. Soudackov, and S. Hammes-Schiffer, “Theoretical modeling of electrochemical proton-coupled electron transfer,” Chem. Rev. (ASAP). DOI: 10.1021/acs.chemrev.1c00929

Structural and thermodynamic effects on the kinetics of C–H oxidation by multisite proton-coupled electron transfer in fluorenyl benzoates

318. B. Koronkiewicz, E. R. Sayfutyarova, S. C. Coste, B. Q. Mercado, S. Hammes-Schiffer, and J. M. Mayer, “Structural and thermodynamic effects on the kinetics of C–H oxidation by multisite proton-coupled electron transfer in fluorenyl benzoates,” J. Org. Chem. 87, 2997-3006 (2022). DOI: 10.1021/acs.joc.1c02834

Multi PCET in symmetrically substituted benzimidazoles

312. E. Odella, M. Secor, M. Elliot, T. L. Groy, T. A. Moore, S. Hammes-Schiffer, and A. L. Moore, “Multi PCET in symmetrically substituted benzimidazoles,” Chem. Sci. 12, 12667-12675 (2021). DOI: 10.1039/D1SC03782J

Multicapacitor approach to interfacial proton-coupled electron transfer thermodynamics at constant potential

311. P. Hutchison, R. E. Warburton, A. V. Soudackov, and S. Hammes-Schiffer, “Multicapacitor approach to interfacial proton-coupled electron transfer thermodynamics at constant potential,” J. Phys. Chem. C 125, 21891-21901 (2021). DOI: 10.1021/acs.jpcc.1c04464

Proton-coupled defects impact O—H bond dissociation free energies on metal oxide surfaces

310. R. E. Warburton, J. M. Mayer, and S. Hammes-Schiffer, “Proton-coupled defects impact O—H bond dissociation free energies on metal oxide surfaces,” J. Phys. Chem. Lett. 12, 9761-9767 (2021). DOI: 10.1021/acs.jpclett.1c02837

Glutamate mediates proton-coupled electron transfer between tyrosines 730 and 731 in Escherichia coli ribonucleotide reductase

301. C. R. Reinhardt, E. Sayfutyarova, J. Zhong, and S. Hammes-Schiffer, “Glutamate mediates proton-coupled electron transfer between tyrosines 730 and 731 in Escherichia coli ribonucleotide reductase,” J. Am. Chem. Soc. 143, 6054-6059 (2021).

The role of intact hydrogen-bond networks in multiproton-coupled electron transfer

294. W. D. Guerra, E. Odella, M. Secor, J. J. Goings, M. N. Urrutia, B. L. Wadsworth, M. Gervaldo, L. E. Sereno, T. A. Moore, G. F. Moore, S. Hammes-Schiffer, and A. L. Moore, “The role of intact hydrogen-bond networks in multiproton-coupled electron transfer,” J. Am. Chem. Soc. 142, 21842-21851 (2020).

Theoretical study of shallow distance dependence of proton-coupled electron transfer in oligoproline metallopeptides

281. P. Li, A. V. Soudackov, B. Koronkiewicz, J. M. Mayer, and S. Hammes-Schiffer, “Theoretical study of shallow distance dependence of proton-coupled electron transfer in oligoproline metallopeptides,” J. Am. Chem. Soc. 142, 13795-13804 (2020).

Proton-coupled electron transfer from tyrosine in the interior of a de novoprotein: Mechanisms and primary proton acceptor

278. A. Nilsen-Moe, C. R. Reinhardt, S. D. Glover, L. Liang, S. Hammes-Schiffer, L. Hammarström, and C. Tommos, “Proton-coupled electron transfer from tyrosine in the interior of a de novoprotein: Mechanisms and primary proton acceptor,” J. Am. Chem. Soc. 142, 11550-11559 (2020).