Role of water in proton-coupled electron transfer between tyrosine and cysteine in ribonucleotide reductase
/in clorice, jiayun, Publications /by Jiayun Zhong325. J. Zhong, C. R. Reinhardt, and S. Hammes-Schiffer, “Role of water in proton-coupled electron transfer between tyrosine and cysteine in ribonucleotide reductase,” J. Am. Chem. Soc. 144, 7208-7214 (2022). DOI: 10.1021/jacs.1c13455
Glutamate mediates proton-coupled electron transfer between tyrosines 730 and 731 in Escherichia coli ribonucleotide reductase
/in clorice, elvira, jiayun, Publications /by Coraline Tao301. 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).
Computing proton-coupled redox potentials of fluorotyrosines in a protein environment
/in clorice, Publications /by Coraline Tao295. C. R. Reinhardt, R. Sequeira, C. Tommos, and S. Hammes-Schiffer, “Computing proton-coupled redox potentials of fluorotyrosines in a protein environment,” J. Phys. Chem. B. 125, 128-136 (2021).
Conformational motions and water networks at the α/β interface in E. coli ribonucleotide reductase
/in clorice, Publications /by Coraline Tao279. C. R. Reinhardt, P. Li, G. Kang, J. Stubbe, C. L. Drennan, and S. Hammes-Schiffer, “Conformational motions and water networks at the α/β interface in E. coli ribonucleotide reductase,” J. Am. Chem. Soc. 142, 13768-13778 (2020).
Proton-coupled electron transfer from tyrosine in the interior of a de novoprotein: Mechanisms and primary proton acceptor
/in clorice, Publications /by Coraline Tao278. 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).
Propensity for proton relay and electrostatic impact of protein reorganization in Slr1694 BLUF photoreceptor
/in clorice, josh, Publications /by Coraline Tao242. J. J. Goings, C. R. Reinhardt, and S. Hammes-Schiffer, “Propensity for proton relay and electrostatic impact of protein reorganization in Slr1694 BLUF photoreceptor,” J. Am. Chem. Soc. 140, 15241-15251 (2018).
Location
Contact
Sharon Hammes-Schiffer
Sterling Professor of Chemistry
Sterling Chemistry Lab, Rm 178
Department of Chemistry
Yale University
225 Prospect Street, PO Box 208107
New Haven, CT 06520-8107
Phone: (203) 436-3936
e-mail: sharon.hammes-schiffer@yale.edu
Tags in Publications
[FeFe]-hydrogenase models [NiFe]-hydrogenase models BLUF catalysis coupled motions Density functional theory treatment Dihydrofolate reductase DNA DNA polymerase electron transfer Electron-proton correlation electrostatics enzyme catalysis Escherichia coli Hartree-Fock HDV ribozyme hydride transfer hydrogen atom transfer hydrogen bonding hydrogen evolution hydrogen tunneling inverted region behavior Ketosteroid Isomerase kinetic isotope effect Liver alcohol dehydrogenase metal ion molecular dynamics molecular electrocatalysts multicomponent density functional theory Nonadiabatic dynamics nonadiabaticity Nuclear quantum effects nuclear-electronic orbital photoinduced proton-coupled electron transfer proton relays Proton transfer proton-coupled electron transfer QM/MM real-time nuclear-electronic orbital reorganization energies ribozyme solvent dynamics Soybean lipoxygenase Surface hopping Vibrational analysis