Long-range electron transfer in heme proteins.

Kinetic experiments have conclusively shown that electron transfer can take place over large distances (greater than 10 angstroms) through protein interiors. Current research focuses on the elucidation of the factors that determine the rates of long-range electron-transfer reactions in modified proteins and protein complexes. Factors receiving experimental and theoretical attention include the donor-acceptor distance, changes in geometry of the donor and acceptor upon electron transfer, and the thermodynamic driving force. Recent experimental work on heme proteins indicates that the electron-transfer rate falls off exponentially with donor-acceptor distance at long range. The rate is greatly enhanced in proteins in which the structural changes accompanying electron transfer are very small.

[1]  T. Poulos,et al.  Models for the complexes formed between cytochrome b5 and the subunits of methemoglobin. , 1983, The Journal of biological chemistry.

[2]  R. Marcus,et al.  Electron transfers in chemistry and biology , 1985 .

[3]  F. Rottman,et al.  Enzymatic synthesis of oligonucleotides of defined sequence: synthesis of a segment of yeast iso-1-cytochrome c gene. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[4]  H. Gray,et al.  Heme-heme orientation and electron transfer kinetic behavior of multisite oxidation-reduction enzymes. , 1983, Science.

[5]  T. Takano,et al.  Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. , 1977, Journal of molecular biology.

[6]  K. Schomacker,et al.  Investigations of the Stokes and anti‐Stokes resonance Raman scattering of cytochrome c , 1984 .

[7]  E. Kosower.  Mechanism of fast intramolecular electron-transfer reactions , 1985 .

[8]  J. Hopfield,et al.  Calculation of tunneling matrix elements in rigid systems: mixed-valence dithiaspirocyclobutane molecules , 1984 .

[9]  E. Margoliash,et al.  The structural gene for yeast cytochrome C. , 1966, Proceedings of the National Academy of Sciences of the United States of America.

[10]  S. S. Isied,et al.  Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[11]  B. Brunschwig,et al.  Configuration changes in electron-exchange reactions of metal complexes , 1982 .

[12]  S. S. Isied,et al.  Electron transfer across polypeptides. III: Oligoproline bridging ligands , 1984 .

[13]  R. Huber,et al.  The structural basis of photosynthetic light reactions in bacteria , 1985 .

[14]  John R. Miller,et al.  Intramolecular long-distance electron transfer in radical anions. The effects of free energy and solvent on the reaction rates , 1984 .

[15]  B. Hoffman,et al.  Electron transfer at crystallographically known long distances (25 .ANG.) in [ZnII,FeIII] hybrid hemoglobin , 1983 .

[16]  H. Gray,et al.  Quenching of zinc-substituted cytochrome c excited states by cytochrome b5 , 1985 .

[17]  John R. Miller,et al.  Fast intramolecular electron transfer in radical ions over long distances across rigid saturated hydrocarbon spacers , 1983 .

[18]  H. Gray,et al.  On the Relationship between Protein-Forced Ligand Fields and the Properties of Blue Copper Centers , 1983 .

[19]  S. Sligar,et al.  Kinetics of cytochrome P-450 reduction: evidence for faster reduction of the high-spin ferric state. , 1985, Biochemistry.

[20]  Richard E. Dickerson,et al.  7 Cytochromes c , 1975 .

[21]  R. Dickerson,et al.  Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution. , 1981, Journal of molecular biology.

[22]  Lester Packer,et al.  Current topics in bioenergetics , 1966 .

[23]  N. Yasuoka,et al.  Refined structure of cytochrome c3 at 1.8 A resolution. , 1984, Journal of molecular biology.

[24]  J. Hopfield,et al.  Limiting forms of the tunneling matrix element in the long distance bridge mediated electron transfer problem , 1985 .

[25]  B. Hall,et al.  Identification and isolation of the yeast cytochrome c gene , 1978, Cell.

[26]  A. D. Gama.  Donor acceptor interaction in metalloproteins , 1985 .

[27]  E. Margoliash,et al.  Long-Range Electron Transfer at Fixed and Known Distance within Protein Complexes , 1985 .

[28]  B. Hoffman,et al.  Temperature dependence of and ligation effects on long-range electron transfer in complementary (zinc,ferric) hemoglobin hybrids , 1986 .

[29]  S. S. Isied,et al.  Electron transfer across polypeptides. 5. Rapid rates of electron transfer between osmium(II) and cobalt(III) in complexes with bridging oligoprolines and other polypeptides , 1985 .

[30]  Arieh Warshel,et al.  On the action of cytochrome c: correlating geometry changes upon oxidation with activation energies of electron transfer , 1983 .

[31]  K. Morokuma,et al.  Stereoelectronic effects in intramolecular long-distance electron transfer in radical anions as predicted by ab-initio MO calculations , 1986 .

[32]  H. Gray,et al.  Long-distance electron transfer in pentaammineruthenium (histidine-48)-myoglobin. Reorganizational energetics of a high-spin heme , 1985 .

[33]  H. Oevering,et al.  Distance dependence of photoinduced electron transfer through non-conjugated bridges , 1985 .

[34]  R. Margalit,et al.  Cytochrome c: a thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters. 1. The effects of temperature, pH and electrostatic media on the standard redox potential of cytochrome c. , 1973, European journal of biochemistry.

[35]  R. Marcus,et al.  A semiclassical model for orientation effects in electron transfer reactions , 1986 .

[36]  T. Takano.  Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale. , 1976, Journal of molecular biology.

[37]  S. S. Isied,et al.  Ruthenium-modified cytochrome c: temperature dependence of the rate of intramolecular electron transfer , 1984 .

[38]  Harry B. Gray,et al.  Electron-transfer kinetics of pentaammineruthenium(III)(histidine-33)-ferricytochrome c. Measurement of the rate of intramolecular electron transfer between redox centers separated by 15.ANG. in a protein , 1982 .

[39]  C. Reed,et al.  Characterization of five-coordinate mono(imidazole)(porphinato)iron(II) complexes , 1985 .

[40]  E. B. Pewitt,et al.  Dependence of rate constants for photoinduced charge separation and dark charge recombination on the free energy of reaction in restricted-distance porphyrin-quinone molecules , 1985 .

[41]  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.

[42]  B. Hoffman,et al.  Temperature dependence of long-range electron transfer in [Zn,FeIII] hybrid hemoglobin , 1984 .

[43]  S. Sligar,et al.  Tyrosine motions in relation to the ferric spin equilibrium of cytochrome P-450cam. , 1985, Biochemistry.

[44]  H. Gray,et al.  Analysis of the kinetics of electron transfer reactions of hemoglobin and myoglobin with inorganic complexes. , 1979, Biochemical and Biophysical Research Communications - BBRC.

[45]  P. Bertrand.  Electron transfer between biological molecules coupled by an exchange interaction , 1985 .

[46]  J. Hopfield,et al.  Failure of the Born–Oppenheimer and Franck–Condon approximations for long distance electron transfer rate calculations , 1984 .

[47]  G. Mclendon,et al.  Long distance electron transfer in polymers and proteins , 1985 .

[48]  J. Onuchic,et al.  Effect of friction on electron transfer in biomolecules , 1985 .

[49]  F R Salemme,et al.  An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b5. , 1976, Journal of molecular biology.

[50]  B Chance,et al.  Studies of photosynthesis using a pulsed laser. I. Temperature dependence of cytochrome oxidation rate in chromatium. Evidence for tunneling. , 1966, Biophysical journal.

[51]  John R. Miller,et al.  The dependence of biological electron transfer rates on exothermicity. The cytochrome c/cytochrome b5 couple , 1985 .

[52]  C. Reed,et al.  Mössbauer and susceptibility study of inter‐heme spin coupling in [Fe (OEP) (2‐MeHIm)]+ dimers , 1985 .

[53]  B. Hall,et al.  Sequence of the gene for iso-l-cytochrome c in saccharomyces cerevisiae , 1979, Cell.

[54]  K. Kadish,et al.  Electrochemical characterization of six-coordinate nitrosyl .sigma.-bonded iron-phenylporphyrins , 1984 .

[55]  D. Lavallee,et al.  Inhibition of thermal electron transfers by the saturated bridging ligand in (.mu.-1,4-dicyanobicyclo[2.2.2]octane)(pentaammineruthenium(II)aquatetraamminecobalt(III) , 1983 .

[56]  J J Hopfield,et al.  Electron transfer between biological molecules by thermally activated tunneling. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[57]  H. Gray.  Centenary Lecture. Long-range electron-transfer in blue copper proteins , 1986 .

[58]  N. Hush.  Distance Dependence of Electron Transfer Rates , 1985 .

[59]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[60]  R. Marcus,et al.  A Model for Orientation Effects in Electron‐Transfer Reactions , 1984 .

[61]  G. Mclendon,et al.  Photoinduced electron transfer within a protein-protein complex formed between physiological redox partners: reduction of ferricytochrome b5 by the hemoglobin derivative .alpha.2Zn.beta.2Fe(III)CN , 1984 .

[62]  H. Inokuchi,et al.  Electrical conduction of hemoprotein in the solid phase: Anhydrous cytochrome c3 film , 1979 .

[63]  J Deisenhofer,et al.  X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. , 1984, Journal of molecular biology.

[64]  E. Margoliash,et al.  Species specificity of long-range electron transfer within the complex between zinc-substituted cytochrome c peroxidase and cytochrome c , 1985 .

[65]  H. Gray,et al.  Kinetics of intermolecular and intramolecular electron transfer from ruthenium(II) complexes to ferricytochrome c , 1984 .

[66]  Y. Hatefi.  The mitochondrial electron transport and oxidative phosphorylation system. , 1985, Annual review of biochemistry.

[67]  J. Kraut,et al.  A hypothetical model of the cytochrome c peroxidase . cytochrome c electron transfer complex. , 1980, The Journal of biological chemistry.