Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2.5 A resolution.
暂无分享,去创建一个
I. Rayment | H. Holden | M. Benning | M. Caffrey | T. Meyer | M. Cusanovich | R. G. Bartsch | G. Wesenberg
[1] F. Daldal,et al. Importance of a conserved hydrogen-bonding network in cytochromes c to their redox potentials and stabilities. , 1991, Biochemistry.
[2] M. Caffrey,et al. The effects of surface charges on the redox potential of cytochrome c2 from the purple phototrophic bacterium Rhodobacter capsulatus. , 1991, Archives of biochemistry and biophysics.
[3] G. Brayer,et al. High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c. , 1990, Journal of molecular biology.
[4] G. Brayer,et al. High-resolution three-dimensional structure of horse heart cytochrome c. , 1990, Journal of molecular biology.
[5] Brian W. Matthews,et al. An efficient general-purpose least-squares refinement program for macromolecular structures , 1987 .
[6] I. Rayment,et al. The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 A resolution. , 1987, The EMBO journal.
[7] I. Rayment,et al. Crystallization and preliminary analysis of crystals of cytochrome c2 from Rhodopseudomonas capsulata. , 1987, Journal of molecular biology.
[8] F. Daldal,et al. Photosynthetic electron transfer in the absence of cytochrome c2 in Rhodopseudomonas capsulata: cytochrome c2 is not essential for electron flow from the cytochrome bc1 complex to the photochemical reaction center , 1986 .
[9] F. Daldal,et al. Cytochrome c(2) is not essential for photosynthetic growth of Rhodopseudomonas capsulata. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[10] J. A. Watkins,et al. Electron transfer between flavodoxin semiquinone and c-type cytochromes: correlations between electrostatically corrected rate constants, redox potentials, and surface topologies. , 1984, Biochemistry.
[11] G. Bhatia. Refinement of the Crystal Structure of Oxidized Rhodospirillum Rubrum Cytochrome C2 , 1984 .
[12] J. A. Watkins,et al. Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[13] David Eisenberg,et al. Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions , 1983 .
[14] R. Dickerson,et al. Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure. , 1981, Journal of molecular biology.
[15] R. Dickerson,et al. Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution. , 1981, Journal of molecular biology.
[16] B. Matthews,et al. An oscillation data collection system for high‐resolution protein crystallography , 1981 .
[17] S. Schichman,et al. A reassessment of the structure of Paracoccus cytochrome c-550. , 1981, Journal of molecular biology.
[18] Michael G. Rossmann,et al. Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting , 1979 .
[19] T. Meyer,et al. Cytochromes C2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria , 1979, Nature.
[20] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[21] N. Xuong,et al. The structure of oxidized cytochrome c 2 of Rhodospirillum rubrum. , 1976, The Journal of biological chemistry.
[22] G. Bricogne,et al. Methods and programs for direct‐space exploitation of geometric redundancies , 1976 .
[23] R. Dickerson,et al. The structure of Paracoccus denitrificans cytochrome c550. , 1976, The Journal of biological chemistry.
[24] P Argos,et al. A comparison of the heme binding pocket in globins and cytochrome b5. , 1975, The Journal of biological chemistry.
[25] A. Schejter,et al. Physicochemical properties of two atypical cytochromes c, Crithidia cytochrome c-557 and Euglena cytochrome c-558. , 1975, The Biochemical journal.
[26] J. Kraut,et al. Structural bases for function in cytochromes c. An interpretation of comparative x-ray and biochemical data. , 1973, The Journal of biological chemistry.
[27] M. Rossmann. The accurate determination of the position and shape of heavy‐atom replacement groups in proteins , 1960 .
[28] M. Caffrey. Characterization of cytochrome c structure and function by site-directed mutagenesis. , 1991 .
[29] G. Tollin,et al. c-Type cytochromes: oxidation-reduction properties. , 1988, Advances in inorganic biochemistry.
[30] T. A. Jones. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. , 1985, Methods in enzymology.
[31] Ivan Rayment,et al. Molecular Replacement Method at Low Resolution: Optimum Strategy and Intrinsic Limitations as Determined by Calculations on Icosahedral Virus Models , 1983 .
[32] T. Meyer,et al. New perspectives on c-type cytochromes. , 1982, Advances in protein chemistry.