Electron transfer from cytochromeb5 to cytochromec
暂无分享,去创建一个
Jill R. Scott | S. Sligar | B. Durham | F. Millett | M. McLean | A. Willie | J. L. Fairris
[1] L. Qin,et al. Photoinduced electron transfer from the triplet state of zinc cytochrome c to ferricytochrome b5 is gated by configurational fluctuations of the diprotein complex. , 1994, Biochemistry.
[2] C. W. Fisher,et al. The high-level expression in Escherichia coli of the membrane-bound form of human and rat cytochrome b5 and studies on their mechanism of function. , 1994, Archives of biochemistry and biophysics.
[3] S. Sligar,et al. Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c. , 1993, Biochemistry.
[4] C. Miller,et al. Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5. , 1993, Biochemistry.
[5] Jill R. Scott,et al. Intramolecular electron transfer in cytochrome b5 labeled with ruthenium(II) polypyridine complexes : rate measurements in the Marcus inverted region , 1993 .
[6] A. Steggles,et al. Differential expression of the mRNAs for the soluble and membrane-bound forms of rabbit cytochrome b5. , 1993, Biochimica et biophysica acta.
[7] G. Tollin,et al. Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex. , 1993, Biochemistry.
[8] S. Sligar,et al. Genetic engineering of redox donor sites: measurement of intracomplex electron transfer between ruthenium-65-cytochrome b5 and cytochrome c. , 1992, Biochemistry.
[9] K. Kalyanasundaram. Photochemistry of Polypyridine and Porphyrin Complexes , 1992 .
[10] G. Brayer,et al. Oxidation state-dependent conformational changes in cytochrome c. , 1992, Journal of molecular biology.
[11] S. Sligar,et al. Mapping electrostatic interactions in macromolecular associations. , 1991, Journal of molecular biology.
[12] G. Tollin,et al. Intra- and intermolecular electron transfer processes in redox proteins. , 1991, Archives of biochemistry and biophysics.
[13] B. Hoffman,et al. Aromatic hole superexchange through position 82 of cytochrome c is not required for intracomplex electron transfer to zinc cytochrome c peroxidase , 1991 .
[14] A. Mauk,et al. Reduction of horse heart ferricytochrome c by bovine liver ferrocytochrome b5. Experimental and theoretical analysis. , 1991, Biochemistry.
[15] R. J. Williams,et al. The formation of protein complexes between ferricytochrome b5 and ferricytochrome c studied using high-resolution 1H-NMR spectroscopy. , 1990, European journal of biochemistry.
[16] B. Durham,et al. Photoinduced electron transfer within complexes between plastocyanin and ruthenium bisbipyridine dicarboxybipyridine cytochrome c derivatives. , 1990, Biochemistry.
[17] N. Borgese,et al. Both the outer mitochondrial membrane and the microsomal forms of cytochrome b5 reductase contain covalently bound myristic acid. Quantitative analysis on the polyvinylidene difluoride-immobilized proteins. , 1990, The Biochemical journal.
[18] G. Moore,et al. NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex. , 1990, Science.
[19] H. Gray,et al. Long-range electron transfer in multisite metalloproteins. , 1989, Biochemistry.
[20] K. Shirabe,et al. Expression of human erythrocyte NADH-cytochrome b5 reductase as an alpha-thrombin-cleavable fused protein in Escherichia coli. , 1989, Biochimica et biophysica acta.
[21] B. Durham,et al. Preparation and characterization of singly labeled ruthenium polypyridine cytochrome c derivatives. , 1988, Biochemistry.
[22] G. Tollin,et al. Kinetics of flavin semiquinone reduction of the components of the cytochrome c-cytochrome b5 complex. , 1988, Biochemistry.
[23] S. Sligar,et al. Probing the mechanisms of macromolecular recognition: the cytochrome b5-cytochrome c complex. , 1988, Science.
[24] G. Mclendon. Long-distance electron transfer in proteins and model systems , 1988 .
[25] J J Wendoloski,et al. Molecular dynamics of a cytochrome c-cytochrome b5 electron transfer complex. , 1987, Science.
[26] P. Weber,et al. Electrostatic analysis of the interaction of cytochrome c with native and dimethyl ester heme substituted cytochrome b5. , 1986, Biochemistry.
[27] John R. Miller,et al. The dependence of biological electron transfer rates on exothermicity. The cytochrome c/cytochrome b5 couple , 1985 .
[28] R. Marcus,et al. Electron transfers in chemistry and biology , 1985 .
[29] M. J. Coon,et al. On the mechanism of action of cytochrome P-450. Oxidation and reduction of the ferrous dioxygen complex of liver microsomal cytochrome P-450 by cytochrome b5. , 1984, The Journal of biological chemistry.
[30] M. R. Mauk,et al. Role of heme propionate groups in cytochrome b5 electron transfer , 1984 .
[31] G. Moore,et al. 1H-n.m.r. investigation of the interaction between cytochrome c and cytochrome b5. , 1983, The Biochemical journal.
[32] F. Lederer,et al. Two homologous cytochromes b5 in a single cell. , 1983, European journal of biochemistry.
[33] H. Gray,et al. Oxidation-reduction equilibrium of cytochrome b5 , 1982 .
[34] M. R. Mauk,et al. Spectrophotometric analysis of the interaction between cytochrome b5 and cytochrome c. , 1982, Biochemistry.
[35] N. Staudenmayer,et al. Use of specific trifluoroacetylation of lysine residues in cytochrome c to study the reaction with cytochrome b5, cytochrome c1, and cytochrome oxidase. , 1980, Biochimica et biophysica acta.
[36] F. Millett,et al. Interaction between cytochrome c and cytochrome b5. , 1979, Biochemistry.
[37] F. Millett,et al. Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. , 1977, Biochemistry.
[38] J. Ozols,et al. Primary structure of the membranous segment of cytochrome b5. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[39] F R Salemme,et al. An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b5. , 1976, Journal of molecular biology.
[40] M. A. Matlib,et al. Properties of rat liver mitochondria with intermembrane Cytochrome c. , 1976, Archives of biochemistry and biophysics.
[41] F. S. Mathews,et al. The structure of ferrocytochrome b5 at 2.8 A resolution. , 1975, The Journal of biological chemistry.
[42] P. Strittmatter,et al. Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. , 1974, Proceedings of the National Academy of Sciences of the United States of America.
[43] P. Strittmatter,et al. A form of reduced nicotinamide adenine dinucleotide-cytochrome b 5 reductase containing both the catalytic site and an additional hydrophobic membrane-binding segment. , 1973, The Journal of biological chemistry.
[44] P. Strittmatter,et al. A form of cytochrome b5 that contains an additional hydrophobic sequence of 40 amino acid residues. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[45] Rudolph A. Marcus,et al. On the Theory of Oxidation‐Reduction Reactions Involving Electron Transfer. I , 1956 .
[46] G. Brayer,et al. Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. , 1994, Biochimie.
[47] S. Sligar,et al. Electron Transfer between Cytochrome B5 Surface Mutants and Cytochrome C , 1991 .
[48] Albert Lester Lehninger,et al. The mitochondrion. Molecular basis of structure and function. , 1964 .