Electrostatic basis for bioenergetics.

作者: Avital Shurki , Marek Štrajbl , Claudia N. Schutz , Arieh Warshel

DOI: 10.1016/S0076-6879(04)80003-X

关键词: ChemistryEnergy metabolismBasis (linear algebra)BioenergeticsBiophysicsStatic electricityProton-Translocating ATPasesHydrogen bond

摘要:

参考文章(101)
W. Cleland, M. Kreevoy, Low-barrier hydrogen bonds and enzymic catalysis Science. ,vol. 264, pp. 1887- 1890 ,(1994) , 10.1126/SCIENCE.8009219
Jordi Villà, Arieh Warshel, Energetics and Dynamics of Enzymatic Reactions Journal of Physical Chemistry B. ,vol. 105, pp. 7887- 7907 ,(2001) , 10.1021/JP011048H
Dmitry A. Cherepanov, Armen Y. Mulkidjanian, Wolfgang Junge, TRANSIENT ACCUMULATION OF ELASTIC ENERGY IN PROTON TRANSLOCATING ATP SYNTHASE FEBS Letters. ,vol. 449, pp. 1- 6 ,(1999) , 10.1016/S0014-5793(99)00386-5
Arpita Yadav, Richard M. Jackson, J. John Holbrook, Arieh Warshel, Role of solvent reorganization energies in the catalytic activity of enzymes Journal of the American Chemical Society. ,vol. 113, pp. 4800- 4805 ,(1991) , 10.1021/JA00013A013
Jan Pieter Abrahams, Andrew GW Leslie, René Lutter, John E Walker, None, Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature. ,vol. 370, pp. 621- 628 ,(1994) , 10.1038/370621A0
P. Arjunan, T. Umland, F. Dyda, S. Swaminathan, W. Furey, M. Sax, B. Farrenkopf, Y. Gao, D. Zhang, F. Jordan, Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. Journal of Molecular Biology. ,vol. 256, pp. 590- 600 ,(1995) , 10.1006/JMBI.1996.0111
Arieh Warshel, Arno Papazyan, Electrostatic effects in macromolecules: fundamental concepts and practical modeling Current Opinion in Structural Biology. ,vol. 8, pp. 211- 217 ,(1998) , 10.1016/S0959-440X(98)80041-9
N. Wu, Y. Mo, J. Gao, E. F. Pai, Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 2017- 2022 ,(2000) , 10.1073/PNAS.050417797