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pro vyhledávání: '"William W. Parson"'
Autor:
William W. Parson
Publikováno v:
The journal of physical chemistry. B. 122(38)
Quantum mechanical/molecular mechanical simulations are used to explore the temperature dependence of intramolecular electron-transfer rates in systems that represent both the “normal” and the “inverted” regions of the Marcus curve. The treat
Publikováno v:
Biochemistry. 42:13673-13683
Effects of ionizable amino acids on spectroscopic properties and electron-transfer kinetics in the photosynthetic reaction center (RC) of Rhodobacter sphaeroides are investigated by site-directed mutations designed to alter the electrostatic environm
Autor:
William W. Parson, Arieh Warshel
Publikováno v:
Quarterly Reviews of Biophysics. 34:563-679
1. Introduction 5632. Obtaining rate constants from molecular-dynamics simulations 5642.1 General relationships between quantum electronic structures and reaction rates 5642.2 The transition-state theory (TST) 5692.3 The transmission coefficient 5723
Publikováno v:
Chemical Physics Letters. 265:293-296
Fushiki and Tachiya [Chem. Phys. Lett. 255 (1996) 83] recently analyzed the free energy surfaces of the initial electron-transfer processes in photosynthetic bacterial reaction centers. The authors state that when the results from simulations describ
Publikováno v:
Proceedings of the National Academy of Sciences. 93:13774-13779
Spectral changes were measured with femtosecond resolution following low-intensity, broad-band excitation of the peripheral antenna complex of the purple photosynthetic bacteriumRhodobacter sphaeroides. Absorption anisotropy decays also were measured
Publikováno v:
Biochemistry. 32:12324-12336
The rates of the light-driven, electron-transfer reactions in the photosynthetic reaction center (RC) of Rhodobacter sphaeroides are examined in mutant strains in which tyrosine (M)210 is replaced by phenylalanine, isoleucine, or tryptophan. The spec
Publikováno v:
ChemInform. 37
Publikováno v:
The Reaction Center of Photosynthetic Bacteria ISBN: 9783642647239
Two approaches for calculating the free energies of transient radical-pair states in bacterial reaction centers are discussed. Although macroscopic models that assign a homogenous dielectric constant to the protein and solvent are major oversimplific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ddb1eb8bbf218b187aae39c420674b8
https://doi.org/10.1007/978-3-642-61157-5_9
https://doi.org/10.1007/978-3-642-61157-5_9
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 91(22)
The effects of multiple changes in hydrogen bond interactions between the electron donor, a bacteriochlorophyll dimer, and histidine residues in the reaction center from Rhodobacter sphaeroides have been investigated. Site-directed mutations were des
Publikováno v:
Biochemistry. 31(33)
The primary electron donor in the reaction center of purple photosynthetic bacteria consists of a pair of bacteriochlorophylls (PL and PM). The oxidized dimer (P+) is expected to have an absorption band in the mid-IR, whose energy and dipole strength