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Volumn 2, Issue 2, 1998, Pages 235-243

Electron transfer mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; DNA; PROTEIN;

EID: 0032039750     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80065-3     Document Type: Article
Times cited : (80)

References (78)
  • 1
    • 0004177528 scopus 로고    scopus 로고
    • BIOS Scientific Publishers; This is a textbook introduction to the experimental and theoretical aspects of protein electron transfer reactions
    • Bendall DS (Ed): Protein Electron Transfer. BIOS Scientific Publishers; 1996. This is a textbook introduction to the experimental and theoretical aspects of protein electron transfer reactions.
    • (1996) Protein Electron Transfer
    • Bendall, D.S.1
  • 2
    • 0000122198 scopus 로고    scopus 로고
    • This is a comprehensive special volume of Chemical Reviews devoted to topics in bioinorganic chemistry, many related to electron transfer proteins
    • Holm RE, Solomon EI (Eds): Chem Rev 1996, 66:2237-3042. This is a comprehensive special volume of Chemical Reviews devoted to topics in bioinorganic chemistry, many related to electron transfer proteins.
    • (1996) Chem Rev , vol.66 , pp. 2237-3042
    • Holm, R.E.1    Solomon, E.I.2
  • 3
    • 85030046082 scopus 로고    scopus 로고
    • This volume contains a wide range of recent chemical, biochemical, electrochemical and theoretical approaches to the electron transfer problem
    • Gray HB (Ed): J Electroanal Chem 1997, 438:1-167. This volume contains a wide range of recent chemical, biochemical, electrochemical and theoretical approaches to the electron transfer problem.
    • (1997) J Electroanal Chem , vol.438 , pp. 1-167
    • Gray, H.B.1
  • 4
    • 0002158284 scopus 로고    scopus 로고
    • This issue contains five commentary articles that discuss the physical and biochemical role played by the protein medium in electron transfer reactions
    • Scott RA (Ed): J Biol lnorg Chem 1997, 2:372-404. This issue contains five commentary articles that discuss the physical and biochemical role played by the protein medium in electron transfer reactions.
    • (1997) J Biol Lnorg Chem , vol.2 , pp. 372-404
    • Scott, R.A.1
  • 5
    • 0032515408 scopus 로고    scopus 로고
    • Side chains affect electron tunneling rates across amino acids
    • Chou T, Chang I-J: Side chains affect electron tunneling rates across amino acids. J Am Chem Soc 1998, 120:227-228.
    • (1998) J am Chem Soc , vol.120 , pp. 227-228
    • Chou, T.1    Chang, I.-J.2
  • 6
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • This summarizes the studies of metal (ruthenium-) modified proteins and their importance for understanding the medium dependence of electron transfer rates. It also highlights secondary structure effects on electron transfer rates and the possible evolutionary consequences
    • Gray HB, Winkler JB: Electron transfer in proteins. Annu Rev Biochem 1996, 65:537-561. This summarizes the studies of metal (ruthenium-) modified proteins and their importance for understanding the medium dependence of electron transfer rates. It also highlights secondary structure effects on electron transfer rates and the possible evolutionary consequences.
    • (1996) Annu Rev Biochem , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.B.2
  • 7
    • 0032507003 scopus 로고    scopus 로고
    • 2(im)(His83)-modified azurin increase below 220 K
    • This reports one of the few modified protein electron transfer (ET) systems that functions to 4 K. Similar to the photosynthetic reaction center, the ET rate actually speeds up (here, by a factor of three to four between 220 K and 170 K) as the temperature is lowered. It is suggested that a reduction in hydrogen bond lengths (along the dominant tunneling pathways) could explain the rate acceleration
    • 2(im)(His83)-modified azurin increase below 220 K. J Am Chem Soc 1998, 120:1102-1103. This reports one of the few modified protein electron transfer (ET) systems that functions to 4 K. Similar to the photosynthetic reaction center, the ET rate actually speeds up (here, by a factor of three to four between 220 K and 170 K) as the temperature is lowered. It is suggested that a reduction in hydrogen bond lengths (along the dominant tunneling pathways) could explain the rate acceleration.
    • (1998) J am Chem Soc , vol.120 , pp. 1102-1103
    • Skov, L.K.1    Pascher, T.2    Winkler, J.R.3    Gray, H.B.4
  • 8
    • 0030663297 scopus 로고    scopus 로고
    • Reorganization energy of blue copper effects of temperature and driving force on the rates of electron transfer in ruthenium and osmium-modified azurins
    • DiBilio AJ, Hill MG, Bonander N, Karlsson BG, Villahermosa RM, Malmström BG, Winkler JR, Gray HB: Reorganization energy of blue copper effects of temperature and driving force on the rates of electron transfer in ruthenium and osmium-modified azurins. J Am Chem Soc 1997, 119;9921-9922.
    • (1997) J am Chem Soc , vol.119 , pp. 9921-9922
    • Dibilio, A.J.1    Hill, M.G.2    Bonander, N.3    Karlsson, B.G.4    Villahermosa, R.M.5    Malmström, B.G.6    Winkler, J.R.7    Gray, H.B.8
  • 10
    • 0031041540 scopus 로고    scopus 로고
    • Computational simulation and analysis of dynamic association between plastocyanin and cytochrome f. Consequences for the electron-transfer reaction
    • Ullmann GM, Knapp EW, Kostic NM: Computational simulation and analysis of dynamic association between plastocyanin and cytochrome f. Consequences for the electron-transfer reaction. J Am Chem Soc 1997, 119:42-52.
    • (1997) J am Chem Soc , vol.119 , pp. 42-52
    • Ullmann, G.M.1    Knapp, E.W.2    Kostic, N.M.3
  • 11
    • 0001102428 scopus 로고    scopus 로고
    • Theory and practice of electron transfer within protein-protein complexes: Application to the multi-domain binding of cytochrome c by cytochrome c peroxidase
    • Nocek JM, Zhou JS, DeForest S, Priyadarshy S, Beratan DN, Onuchic JN, Hoffman BM: Theory and practice of electron transfer within protein-protein complexes: application to the multi-domain binding of cytochrome c by cytochrome c peroxidase. Chem Rev 1996, 96:2459-2489.
    • (1996) Chem Rev , vol.96 , pp. 2459-2489
    • Nocek, J.M.1    Zhou, J.S.2    Deforest, S.3    Priyadarshy, S.4    Beratan, D.N.5    Onuchic, J.N.6    Hoffman, B.M.7
  • 12
    • 0000421196 scopus 로고    scopus 로고
    • Ab initio based effective hamiltonians for long range electron transfer. Hartree-Fock analysis
    • Kurnikov IV, Beratan DN. Ab initio based effective hamiltonians for long range electron transfer. Hartree-Fock analysis. J Chem Phys 1996, 105:9571-9573.
    • (1996) J Chem Phys , vol.105 , pp. 9571-9573
    • Kurnikov, I.V.1    Beratan, D.N.2
  • 13
    • 0002710288 scopus 로고    scopus 로고
    • Protein-mediated electron transfer: Pathways, orbital interactions and contact maps
    • Edited by Canters GW, Vijgenboom E. Dordrecht: Kluwer Academic Publishers; in press
    • Beratan DN, Skourtis SS: Protein-mediated electron transfer: pathways, orbital interactions and contact maps. In Biological electron transfer chains: genetics, composition and mode of operation. Edited by Canters GW, Vijgenboom E. Dordrecht: Kluwer Academic Publishers; 1998:in press.
    • (1998) Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation
    • Beratan, D.N.1    Skourtis, S.S.2
  • 14
    • 0030806879 scopus 로고    scopus 로고
    • High and low resolution theories of protein electron transfer
    • Skourtis SS, Beratan DN: High and low resolution theories of protein electron transfer. J Biol Inorg Chem 1997, 2:378-386.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 378-386
    • Skourtis, S.S.1    Beratan, D.N.2
  • 15
    • 0029612224 scopus 로고
    • The currents of life -the terminal electron transfer complex of respiration
    • Ramirez BE, Malmström BG, Gray HB: The currents of life -the terminal electron transfer complex of respiration. Proc Natl Acad Sci USA 1995, 92:11949-11951.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11949-11951
    • Ramirez, B.E.1    Malmström, B.G.2    Gray, H.B.3
  • 16
    • 0030744604 scopus 로고    scopus 로고
    • Biological electron tunneling through native protein media
    • Winkler JR, Gray HB: Biological electron tunneling through native protein media. J Biol Inorg Chem 1997, 2:399-404.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 399-404
    • Winkler, J.R.1    Gray, H.B.2
  • 17
    • 0030810994 scopus 로고    scopus 로고
    • Electron tunneling in proteins: Role of the intervening medium
    • Moser CC, Page CC, Chen X, Dutton PL: Electron tunneling in proteins: role of the intervening medium. J Biol Inorg Chem 1997, 2:393-398.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 393-398
    • Moser, C.C.1    Page, C.C.2    Chen, X.3    Dutton, P.L.4
  • 18
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 1.8Å
    • This paper describes the recent three-dimensional structure of cytochrome c oxidase
    • Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawaitoh K, Nakashima R, Yaono R, Yoshikawa S. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 1.8Å. Science 1996, 272:1136-1144. This paper describes the recent three-dimensional structure of cytochrome c oxidase.
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3    Tomizaki, T.4    Yamaguchi, H.5    Shinzawaitoh, K.6    Nakashima, R.7    Yaono, R.8    Yoshikawa, S.9
  • 20
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Describes the structure and function of ATP synthase, the biological machine that transforms ionic gradients into chemical bonds
    • Boyer PD: The ATP synthase - a splendid molecular machine. Annu Rev Biochem 1997, 66:717-749. Describes the structure and function of ATP synthase, the biological machine that transforms ionic gradients into chemical bonds.
    • (1997) Annu Rev Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 21
    • 0031033975 scopus 로고    scopus 로고
    • Conversion of light energy to proton potential in liposomes by artificial photosynthetic reaction centers
    • An example of an artificial system that transforms photons into a transmembrane ion gradient
    • Steinberg-Yfrach G, Liddell PA, Hung SC, Moore AL, Gust D, Moore TA: Conversion of light energy to proton potential in liposomes by artificial photosynthetic reaction centers. Nature 1997, 385:239-241. An example of an artificial system that transforms photons into a transmembrane ion gradient.
    • (1997) Nature , vol.385 , pp. 239-241
    • Steinberg-Yfrach, G.1    Liddell, P.A.2    Hung, S.C.3    Moore, A.L.4    Gust, D.5    Moore, T.A.6
  • 22
    • 0032473977 scopus 로고    scopus 로고
    • 1 ATP-synthase in an artificial photosynthetic membrane
    • 1 ATP synthase has been incorporated into liposomes containing chromophores that undergo light driven electron transfer (ET) and coupled proton transfer. With a quantum yield of >7%, the system uses light to drive the chemical synthesis of ATP and ADP. This is perhaps the first artificial system to couple fully photoinduced ET to the generation of an electrochemical gradient and the endothermic formation of chemical bonds
    • 1 ATP synthase has been incorporated into liposomes containing chromophores that undergo light driven electron transfer (ET) and coupled proton transfer. With a quantum yield of >7%, the system uses light to drive the chemical synthesis of ATP and ADP. This is perhaps the first artificial system to couple fully photoinduced ET to the generation of an electrochemical gradient and the endothermic formation of chemical bonds.
    • (1998) Nature , vol.392 , pp. 479-482
    • Steinberg-Yfrach, G.1    Rigaud, J.L.2    Duranti, E.N.3    Moore, A.L.4    Gust, D.5    Moore, T.A.6
  • 23
    • 0031260356 scopus 로고    scopus 로고
    • Significant effect of salt bridges on electron-transfer
    • Kirby JP, Roberts JA, Nocera DG: Significant effect of salt bridges on electron-transfer. J Am Chem Soc 1997, 119:9230-9236.
    • (1997) J am Chem Soc , vol.119 , pp. 9230-9236
    • Kirby, J.P.1    Roberts, J.A.2    Nocera, D.G.3
  • 24
    • 0007833593 scopus 로고    scopus 로고
    • Synthesis of (porphinato) zinc(II) - Spacer - (porphinato) iron(III) chloride complexes. a modular approach to fixed-distance electron-transfer model compounds through the efficacy of metal-mediated cross-coupling
    • DeRege PJF, Therien MJ: Synthesis of (porphinato) zinc(II) - spacer - (porphinato) iron(III) chloride complexes. A modular approach to fixed-distance electron-transfer model compounds through the efficacy of metal-mediated cross-coupling. Inorg Chim Acta 1996, 242:211-218.
    • (1996) Inorg Chim Acta , vol.242 , pp. 211-218
    • Derege, P.J.F.1    Therien, M.J.2
  • 26
    • 0001409808 scopus 로고    scopus 로고
    • Electronic coupling in C-clamp-shaped molecules - Solvent-mediated superexchange pathways
    • Kumar K, Lin Z, Waldeck DH, Zimmt MB: Electronic coupling in C-clamp-shaped molecules - solvent-mediated superexchange pathways. J Am Chem Soc 1996, 118:243-244.
    • (1996) J am Chem Soc , vol.118 , pp. 243-244
    • Kumar, K.1    Lin, Z.2    Waldeck, D.H.3    Zimmt, M.B.4
  • 27
    • 0029880595 scopus 로고    scopus 로고
    • Conformational dependence of electron transfer across de novo designed metalloproteins
    • Gretchikhine AB, Ogawa MY: Conformational dependence of electron transfer across de novo designed metalloproteins. J Am Chem Soc 1996, 118:1543-1544.
    • (1996) J am Chem Soc , vol.118 , pp. 1543-1544
    • Gretchikhine, A.B.1    Ogawa, M.Y.2
  • 29
    • 0030590514 scopus 로고    scopus 로고
    • Synthesis of a β-turn forming depsipeptide for hydrogen-bond mediated electron-transfer studies
    • Williamson DA, Bowler BE: Synthesis of a β-turn forming depsipeptide for hydrogen-bond mediated electron-transfer studies. Tetrahedron 1996, 52:12357-12372.
    • (1996) Tetrahedron , vol.52 , pp. 12357-12372
    • Williamson, D.A.1    Bowler, B.E.2
  • 31
    • 0029931828 scopus 로고    scopus 로고
    • Effect of the electric field generated by the helix dipole on photoinduced intramolecular electron transfer in dichromophoric alpha-helical peptides
    • Galoppini E, Fox MA: Effect of the electric field generated by the helix dipole on photoinduced intramolecular electron transfer in dichromophoric alpha-helical peptides. J Am Chem Soc 1996, 118:2299-2300.
    • (1996) J am Chem Soc , vol.118 , pp. 2299-2300
    • Galoppini, E.1    Fox, M.A.2
  • 32
    • 0030859221 scopus 로고    scopus 로고
    • Electric field effects on electron transfer rates in dichromophoric peptides - The effect of helix unfolding
    • Galoppini E, Fox MA: Electric field effects on electron transfer rates in dichromophoric peptides - the effect of helix unfolding. J Am Chem Soc 1997, 119:5277-5285.
    • (1997) J am Chem Soc , vol.119 , pp. 5277-5285
    • Galoppini, E.1    Fox, M.A.2
  • 33
    • 0030738770 scopus 로고    scopus 로고
    • Differential control of intramolecular charge separation and recombination rates using nematic liquid-crystal solvents
    • Wiederrecht GP, Svec WA, Wasielewski MR: Differential control of intramolecular charge separation and recombination rates using nematic liquid-crystal solvents. J Am Chem Soc 1997, 119:6199-6200.
    • (1997) J am Chem Soc , vol.119 , pp. 6199-6200
    • Wiederrecht, G.P.1    Svec, W.A.2    Wasielewski, M.R.3
  • 34
    • 0031210512 scopus 로고    scopus 로고
    • How nature harvests sunlight
    • Hu X, Schulten K: How nature harvests sunlight Phys Today 1997, 50:28-34.
    • (1997) Phys Today , vol.50 , pp. 28-34
    • Hu, X.1    Schulten, K.2
  • 37
    • 0031590080 scopus 로고    scopus 로고
    • Estimating the effect of protein dynamics on electron transfer to the special pair in the photosynthetic reaction center
    • Aquino AJA, Beroza P, Regan J, Onuchic JN: Estimating the effect of protein dynamics on electron transfer to the special pair in the photosynthetic reaction center. Chem Phys Lett 1997, 275:181-187.
    • (1997) Chem Phys Lett , vol.275 , pp. 181-187
    • Aquino, A.J.A.1    Beroza, P.2    Regan, J.3    Onuchic, J.N.4
  • 38
    • 0030468363 scopus 로고    scopus 로고
    • Effects of mutations in plastocyanin on the kinetics of the protein rearrangement gating the electron-transfer reaction with zinc cytochrome c. Analysis of the rearrangement pathway
    • Crnogorac MM, Shen CY, Young S, Hansson O, Kostic NM: Effects of mutations in plastocyanin on the kinetics of the protein rearrangement gating the electron-transfer reaction with zinc cytochrome c. Analysis of the rearrangement pathway. Biochemistry 1996, 35:16465-16474.
    • (1996) Biochemistry , vol.35 , pp. 16465-16474
    • Crnogorac, M.M.1    Shen, C.Y.2    Young, S.3    Hansson, O.4    Kostic, N.M.5
  • 39
  • 41
    • 0029827310 scopus 로고    scopus 로고
    • Optical control of photogenerated ion-pair lifetimes - An approach to a molecular switch
    • Debreczeny MP, Svec WA, Wasielewski MR: Optical control of photogenerated ion-pair lifetimes - an approach to a molecular switch. Science 1996, 274:584-587.
    • (1996) Science , vol.274 , pp. 584-587
    • Debreczeny, M.P.1    Svec, W.A.2    Wasielewski, M.R.3
  • 42
    • 0029841859 scopus 로고    scopus 로고
    • Femtosecond optical control of charge shift within electron donor-acceptor arrays - An approach to molecular switches
    • Debreczeny MP, Svec WA, Marsh EM, Wasielewski M: Femtosecond optical control of charge shift within electron donor-acceptor arrays - an approach to molecular switches. J Am Chem Soc 1996, 118:8174-8175.
    • (1996) J am Chem Soc , vol.118 , pp. 8174-8175
    • Debreczeny, M.P.1    Svec, W.A.2    Marsh, E.M.3    Wasielewski, M.4
  • 43
    • 0003645650 scopus 로고    scopus 로고
    • Oxford: Blackwell Science; 1997. The most up-to-date textbook that connects electron transfer processes to molecular scale electronic devices
    • st century monograph. Oxford: Blackwell Science; 1997. The most up-to-date textbook that connects electron transfer processes to molecular scale electronic devices.
    • st Century Monograph
    • Jortner, J.1    Ratner, M.2
  • 47
    • 0029846245 scopus 로고    scopus 로고
    • Rates of DNA-mediated electron transfer between metallointercalators
    • Describes the kinetics of ET systems with a range of donor-acceptor systems
    • Arkin MR, Stemp EDA, Holmlin RE, Barton JK, Hoermann A, Olson EJC, Barbara PF: Rates of DNA-mediated electron transfer between metallointercalators. Science 1996, 273:9230-9236. Describes the kinetics of ET systems with a range of donor-acceptor systems.
    • (1996) Science , vol.273 , pp. 9230-9236
    • Arkin, M.R.1    Stemp, E.D.A.2    Holmlin, R.E.3    Barton, J.K.4    Hoermann, A.5    Olson, E.J.C.6    Barbara, P.F.7
  • 49
    • 0030951374 scopus 로고    scopus 로고
    • 3+ to DNA
    • This paper points to spectroscopic evidence for cooperative donor-acceptor binding in DNA
    • 3+ to DNA. J Am Chem Soc 1997, 119:1454-1455. This paper points to spectroscopic evidence for cooperative donor-acceptor binding in DNA.
    • (1997) J am Chem Soc , vol.119 , pp. 1454-1455
    • Lincoln, P.1    Tuite, E.2    Norden, B.3
  • 50
    • 0012655895 scopus 로고    scopus 로고
    • DNa is not a molecular wire: Protein-like electron-transfer predicted for an extended pi-electron system
    • Theoretical analysis predicts the range of electron transfer in DNA should be similar to that found earlier in proteins for similar donor and acceptor redox potentials
    • Priyadarshy S, Risser SM, Beratan DN: DNA is not a molecular wire: protein-like electron-transfer predicted for an extended pi-electron system. J Phys Chem 1996, 100:17678-17682. Theoretical analysis predicts the range of electron transfer in DNA should be similar to that found earlier in proteins for similar donor and acceptor redox potentials.
    • (1996) J Phys Chem , vol.100 , pp. 17678-17682
    • Priyadarshy, S.1    Risser, S.M.2    Beratan, D.N.3
  • 51
    • 0030820847 scopus 로고    scopus 로고
    • Distance-dependent electron transfer in DNA hairpins
    • The first report of electron transfer rates in DNA systems with systematically varied donor-acceptor distances. The crucial advances are the limited motional freedom of the donor and acceptor groups, and the possibility of varying their positions to sample a range of distances
    • Lewis FD, Wu TF, Zhang YF, Letsinger RL, Greenfield SR, Wasielewski MR: Distance-dependent electron transfer in DNA hairpins. Science 1997, 277:673-676. The first report of electron transfer rates in DNA systems with systematically varied donor-acceptor distances. The crucial advances are the limited motional freedom of the donor and acceptor groups, and the possibility of varying their positions to sample a range of distances.
    • (1997) Science , vol.277 , pp. 673-676
    • Lewis, F.D.1    Wu, T.F.2    Zhang, Y.F.3    Letsinger, R.L.4    Greenfield, S.R.5    Wasielewski, M.R.6
  • 52
    • 0031209440 scopus 로고    scopus 로고
    • Electron-transfer rates in bridged molecular-systems. a phenomenological approach to relaxation
    • Davis WB, Wasielewski MR, Ratner MA, Mujica V, Nitzan A: Electron-transfer rates in bridged molecular-systems. A phenomenological approach to relaxation. J Phys Chem 1997, 101:6158-6164.
    • (1997) J Phys Chem , vol.101 , pp. 6158-6164
    • Davis, W.B.1    Wasielewski, M.R.2    Ratner, M.A.3    Mujica, V.4    Nitzan, A.5
  • 53
    • 0031906759 scopus 로고    scopus 로고
    • Distance dependence of photoinduced electron-transfer in DNA
    • Fukui K, Tanaka K: Distance dependence of photoinduced electron-transfer in DNA. Agnew Chem Int Ed 1998, 37:158-161.
    • (1998) Agnew Chem int Ed , vol.37 , pp. 158-161
    • Fukui, K.1    Tanaka, K.2
  • 54
    • 0029833916 scopus 로고    scopus 로고
    • Oxidative DNA damage through long-range electron transfer
    • Hall DB, Holmlin RE, Barton JK: Oxidative DNA damage through long-range electron transfer. Nature 1997, 382:731-735.
    • (1997) Nature , vol.382 , pp. 731-735
    • Hall, D.B.1    Holmlin, R.E.2    Barton, J.K.3
  • 55
    • 1842330888 scopus 로고    scopus 로고
    • Oxidative thymine dimer repair in the DNA helix
    • Dandliker PJ, Holmlin RE, Barton JK: Oxidative thymine dimer repair in the DNA helix. Science 1997, 275:1465-1468.
    • (1997) Science , vol.275 , pp. 1465-1468
    • Dandliker, P.J.1    Holmlin, R.E.2    Barton, J.K.3
  • 56
    • 0000707810 scopus 로고    scopus 로고
    • Bridge-mediated electronic interactions: Difference between hamiltonian and green function partitioning in a non-orthogonal basis
    • Priyadarshy S, Skourtis SS, Risser SM, Beratan DN: Bridge-mediated electronic interactions: difference between hamiltonian and green function partitioning in a non-orthogonal basis. J Chem Phys 1996, 104:9473-9481.
    • (1996) J Chem Phys , vol.104 , pp. 9473-9481
    • Priyadarshy, S.1    Skourtis, S.S.2    Risser, S.M.3    Beratan, D.N.4
  • 57
    • 0031566913 scopus 로고    scopus 로고
    • On the non-orthogonal basis-set calculations of the bridge-mediated electronic matrix elements
    • Stuchebrukhov AA: On the non-orthogonal basis-set calculations of the bridge-mediated electronic matrix elements. Chem Phys Lett 1997, 265:643-648.
    • (1997) Chem Phys Lett , vol.265 , pp. 643-648
    • Stuchebrukhov, A.A.1
  • 58
    • 5244336175 scopus 로고    scopus 로고
    • Calculation of electronic tunnel matrix elements in proteins. Comparison of exact and approximate one-electron methods for Ru-modified azurin
    • Daizadeh I, Gehlen JN, Stuchebrukhov AA: Calculation of electronic tunnel matrix elements in proteins. Comparison of exact and approximate one-electron methods for Ru-modified azurin. J Chem Phys 1997, 106:5658-5666.
    • (1997) J Chem Phys , vol.106 , pp. 5658-5666
    • Daizadeh, I.1    Gehlen, J.N.2    Stuchebrukhov, A.A.3
  • 59
    • 28244468463 scopus 로고    scopus 로고
    • Tunneling currents in electron-transfer reactions in proteins
    • Stuchebrukhov AA: Tunneling currents in electron-transfer reactions in proteins. J Chem Phys 1996; 104:8424-8432.
    • (1996) J Chem Phys , vol.104 , pp. 8424-8432
    • Stuchebrukhov, A.A.1
  • 60
    • 4243234418 scopus 로고    scopus 로고
    • Calculation of electronic coupling matrix-elements for ground and excited state electron-transfer reactions. Comparison of the generalized Mulliken-Hush and block diagonalization methods
    • Cave RJ, Newton MD: Calculation of electronic coupling matrix-elements for ground and excited state electron-transfer reactions. Comparison of the generalized Mulliken-Hush and block diagonalization methods. J Chem Phys 1997, 106:9213-9226.
    • (1997) J Chem Phys , vol.106 , pp. 9213-9226
    • Cave, R.J.1    Newton, M.D.2
  • 61
    • 0030180687 scopus 로고    scopus 로고
    • Connection between simple-models and quantum-chemical models for electron-transfer tunneling matrix element calculations. A Dyson's equations-based approach
    • Balabiin IA, Onuchic JN: Connection between simple-models and quantum-chemical models for electron-transfer tunneling matrix element calculations. A Dyson's equations-based approach. J Phys Chem 1996, 100:11573-11580.
    • (1996) J Phys Chem , vol.100 , pp. 11573-11580
    • Balabiin, I.A.1    Onuchic, J.N.2
  • 62
    • 0030859229 scopus 로고    scopus 로고
    • Through-bond orbital coupling, the parity rule, and the design of superbridges which exhibit greatly enhanced electronic coupling. A natural bond orbital analysis
    • Paddon-Row MN, Shephard MJ: Through-bond orbital coupling, the parity rule, and the design of superbridges which exhibit greatly enhanced electronic coupling. A natural bond orbital analysis. J Am Chem Soc 1997, 119:5355-5365.
    • (1997) J am Chem Soc , vol.119 , pp. 5355-5365
    • Paddon-Row, M.N.1    Shephard, M.J.2
  • 63
    • 0031559366 scopus 로고    scopus 로고
    • Ab initio quantum-chemical calculation of electron-transfer matrix-elements for large molecules
    • Zhang LY, Friesner RA, Murphy RB: Ab initio quantum-chemical calculation of electron-transfer matrix-elements for large molecules. J Chem Phys 1997, 107:450-459.
    • (1997) J Chem Phys , vol.107 , pp. 450-459
    • Zhang, L.Y.1    Friesner, R.A.2    Murphy, R.B.3
  • 64
    • 4143104515 scopus 로고    scopus 로고
    • Semiempirical molecular-orbital calculations with linear-system size scaling
    • Dixon SL, Merz KM: Semiempirical molecular-orbital calculations with linear-system size scaling. J Chem Phys 1996, 104:6643-6649.
    • (1996) J Chem Phys , vol.104 , pp. 6643-6649
    • Dixon, S.L.1    Merz, K.M.2
  • 65
    • 0013357779 scopus 로고    scopus 로고
    • Linear scaling semiempirical quantum calculations for macromolecules
    • Lee TS, York DM, Yang WT: Linear scaling semiempirical quantum calculations for macromolecules. J Chem Phys 1996, 105:2744-2750.
    • (1996) J Chem Phys , vol.105 , pp. 2744-2750
    • Lee, T.S.1    York, D.M.2    Yang, W.T.3
  • 66
    • 0031075543 scopus 로고    scopus 로고
    • Electron transfer contact maps
    • This presents a systematic strategy for developing reduced views of electronic interactions in proteins. The strategy is of particular use for analyzing the role of protein motifs in ET, and the influence of protein motion upon electronic propagation
    • Skourtis SS, Beratan DN: Electron transfer contact maps. J Phys Chem B 1996, 101:1215-1234. This presents a systematic strategy for developing reduced views of electronic interactions in proteins. The strategy is of particular use for analyzing the role of protein motifs in ET, and the influence of protein motion upon electronic propagation.
    • (1996) J Phys Chem B , vol.101 , pp. 1215-1234
    • Skourtis, S.S.1    Beratan, D.N.2
  • 67
    • 0030806879 scopus 로고    scopus 로고
    • High and low resolution theories of protien electron transfer
    • Skourtis SS, Beratan DN: High and low resolution theories of protien electron transfer. J Biol Inorg Chem 1997, 2:378-386.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 378-386
    • Skourtis, S.S.1    Beratan, D.N.2
  • 69
    • 0000564578 scopus 로고    scopus 로고
    • Secondary structure conformations and long range electronic interactions in oligopeptides
    • Wolfgang J, Risser SM, Priyadarshy S, Beratan DN: Secondary structure conformations and long range electronic interactions in oligopeptides. J Phys Chem B 1997, 101:2986-2991.
    • (1997) J Phys Chem B , vol.101 , pp. 2986-2991
    • Wolfgang, J.1    Risser, S.M.2    Priyadarshy, S.3    Beratan, D.N.4
  • 71
    • 0030578036 scopus 로고    scopus 로고
    • Control of dynamics of a dissipative two-level system by a strong periodic field
    • Goychuk IA, Petrov EG, May V: Control of dynamics of a dissipative two-level system by a strong periodic field. Chem Phys Lett 1996, 253:428-437.
    • (1996) Chem Phys Lett , vol.253 , pp. 428-437
    • Goychuk, I.A.1    Petrov, E.G.2    May, V.3
  • 72
    • 0030588777 scopus 로고    scopus 로고
    • Dynamic effects in non-adiabatic charge transfer
    • Gudkowska-Nowak E: Dynamic effects in non-adiabatic charge transfer. Chem Phys 1996, 212:115-123.
    • (1996) Chem Phys , vol.212 , pp. 115-123
    • Gudkowska-Nowak, E.1
  • 73
    • 0031559805 scopus 로고    scopus 로고
    • Inelastic tunneling in long-distance biological electron transfer reactions
    • Medvedev ES, Stuchebrukhov AA: Inelastic tunneling in long-distance biological electron transfer reactions. J Chem Phys 1997, 107:3821-3831.
    • (1997) J Chem Phys , vol.107 , pp. 3821-3831
    • Medvedev, E.S.1    Stuchebrukhov, A.A.2
  • 74
    • 0041039677 scopus 로고    scopus 로고
    • Resonance interference in a 3-level system with dynamic coupling of the intermediate state to a vibrational-mode
    • Kuznetsov AM, Ulstrup J: Resonance interference in a 3-level system with dynamic coupling of the intermediate state to a vibrational-mode. Mol Phys 1996, 87:1189-1197.
    • (1996) Mol Phys , vol.87 , pp. 1189-1197
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 75
    • 0008158666 scopus 로고    scopus 로고
    • Energetics of the primary charge separation in bacterial photosynthesis
    • Edited by Michel-Beyerle ME. New York: Springer Verlag
    • Bixon M, Jortner J, Michel-Beyerle ME: Energetics of the primary charge separation in bacterial photosynthesis. In Reaction centers of photosynthetic bacteria. Edited by Michel-Beyerle ME. New York: Springer Verlag; 1996:287-296.
    • (1996) Reaction Centers of Photosynthetic Bacteria , pp. 287-296
    • Bixon, M.1    Jortner, J.2    Michel-Beyerle, M.E.3
  • 76
    • 0008843559 scopus 로고    scopus 로고
    • Three state model for two-electron transfer reactions
    • Zusman LD, Beratan DN: Three state model for two-electron transfer reactions. J Phys Chem A 1997, 101:4136-4141.
    • (1997) J Phys Chem A , vol.101 , pp. 4136-4141
    • Zusman, L.D.1    Beratan, D.N.2
  • 77
    • 0001726244 scopus 로고    scopus 로고
    • N2 reactions and relation to those of outer-sphere bond rupture electron transfers
    • N2 reactions and relation to those of outer-sphere bond rupture electron transfers. J Phys Chem A 1997, 101:4072-4087.
    • (1997) J Phys Chem A , vol.101 , pp. 4072-4087
    • Marcus, R.A.1
  • 78
    • 0030453048 scopus 로고    scopus 로고
    • Multidimensional Marcus theory. An analysis of concerted reactions
    • Guthrie JP: Multidimensional Marcus theory. An analysis of concerted reactions. J Am Chem Soc 1996, 118:12878-12885.
    • (1996) J am Chem Soc , vol.118 , pp. 12878-12885
    • Guthrie, J.P.1


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