메뉴 건너뛰기




Volumn 12, Issue 6, 2008, Pages 755-759

Electron transfer in peptides and proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYTOCHROME; HISTIDINE; PEPTIDE; PHENOL; PROTEIN; RIBONUCLEOTIDE REDUCTASE; RUTHENIUM; TYROSINE;

EID: 57549111042     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2008.08.026     Document Type: Review
Times cited : (103)

References (42)
  • 1
    • 33748216903 scopus 로고
    • Electron transfer reactions in chemistry: theory and experiment (Nobel Lecture)
    • Marcus R.A. Electron transfer reactions in chemistry: theory and experiment (Nobel Lecture). Angew Chem Int Ed Engl 32 (1993) 1111
    • (1993) Angew Chem Int Ed Engl , vol.32 , pp. 1111
    • Marcus, R.A.1
  • 2
    • 0016273342 scopus 로고
    • Electron transfer between biological molecules by thermally activated tunneling
    • Hopfield J.J. Electron transfer between biological molecules by thermally activated tunneling. Proc Natl Acad Sci U S A 71 (1974) 3640-3644
    • (1974) Proc Natl Acad Sci U S A , vol.71 , pp. 3640-3644
    • Hopfield, J.J.1
  • 4
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunneling through proteins
    • Gray H.B., and Winkler J.R. Electron tunneling through proteins. Q Rev Biophys 36 (2003) 341-372
    • (2003) Q Rev Biophys , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 6
    • 33846849448 scopus 로고    scopus 로고
    • Coupling coherence distinguishes structure sensitivity in protein electron transfer
    • This paper shows the importance of the pathway model for the description of long-distance ET in proteins.
    • Prytkova T.R., Kurnikov I.V., and Beratan D.N. Coupling coherence distinguishes structure sensitivity in protein electron transfer. Science 315 (2007) 622-625. This paper shows the importance of the pathway model for the description of long-distance ET in proteins.
    • (2007) Science , vol.315 , pp. 622-625
    • Prytkova, T.R.1    Kurnikov, I.V.2    Beratan, D.N.3
  • 7
    • 0040960707 scopus 로고
    • Electron tunneling through covalent and noncovalent pathways
    • Beratan D.N., Onuchic J.N., and Hopfield J.J. Electron tunneling through covalent and noncovalent pathways. J Phys Chem 86 (1987) 4488-4498
    • (1987) J Phys Chem , vol.86 , pp. 4488-4498
    • Beratan, D.N.1    Onuchic, J.N.2    Hopfield, J.J.3
  • 8
    • 14844351561 scopus 로고    scopus 로고
    • Protein dynamics and electron transfer: electronic decoherence and non-Condon effects
    • Skourtis S.S., Balabin I.A., Kawatsu T., and Beratan D.N. Protein dynamics and electron transfer: electronic decoherence and non-Condon effects. Proc Natl Acad Sci U S A 102 (2005) 3525-3557
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3525-3557
    • Skourtis, S.S.1    Balabin, I.A.2    Kawatsu, T.3    Beratan, D.N.4
  • 9
    • 38649102135 scopus 로고    scopus 로고
    • Heme-copper oxidases use tunneling pathways
    • Beratan D.N., and Balabin I.A. Heme-copper oxidases use tunneling pathways. Proc Natl Acad Sci U S A 105 (2008) 403-404
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 403-404
    • Beratan, D.N.1    Balabin, I.A.2
  • 10
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X.X., and Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402 (1999) 47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 11
    • 33748343422 scopus 로고    scopus 로고
    • Darwin at the molecular scale: selection and variance in electron tunnelling proteins including cytochrome c oxidase
    • This paper argues against a specific design of ET pathways in proteins.
    • Moser C.C., Page C.C., and Dutton L.P. Darwin at the molecular scale: selection and variance in electron tunnelling proteins including cytochrome c oxidase. Phil Trans R Soc B 361 (2006) 1295-1305. This paper argues against a specific design of ET pathways in proteins.
    • (2006) Phil Trans R Soc B , vol.361 , pp. 1295-1305
    • Moser, C.C.1    Page, C.C.2    Dutton, L.P.3
  • 12
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • Page C.C., Moser C.C., and Dutton L.P. Mechanism for electron transfer within and between proteins. Curr Opin Chem Biol 7 (2003) 551-556
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, L.P.3
  • 13
    • 0038208381 scopus 로고    scopus 로고
    • Radical initiation in the class I ribonucleotide reductase: long-range proton coupled electron transfer
    • Stubbe J., Nocera D.G., Yee C.S., and Chang M.C.Y. Radical initiation in the class I ribonucleotide reductase: long-range proton coupled electron transfer. Chem Rev 103 (2003) 2167-2201
    • (2003) Chem Rev , vol.103 , pp. 2167-2201
    • Stubbe, J.1    Nocera, D.G.2    Yee, C.S.3    Chang, M.C.Y.4
  • 14
    • 36849004028 scopus 로고    scopus 로고
    • 731 in radical propagation
    • This paper describes the importance of Tyr730 and Tyr731 as hopping relays for ET through ribonucleotide reductase.
    • 731 in radical propagation. J Am Chem Soc 129 (2007) 15060-15071. This paper describes the importance of Tyr730 and Tyr731 as hopping relays for ET through ribonucleotide reductase.
    • (2007) J Am Chem Soc , vol.129 , pp. 15060-15071
    • Seyedsayamdost, M.R.1    Xie, J.2    Chan, C.T.Y.3    Schultz, P.G.4    Stubbe, J.5
  • 15
    • 33847666363 scopus 로고    scopus 로고
    • 356DOPA-β2 heterodimer of E. coli ribonucleotide reductase
    • 356DOPA-β2 heterodimer of E. coli ribonucleotide reductase. J Am Chem Soc 129 (2007) 2226-2227
    • (2007) J Am Chem Soc , vol.129 , pp. 2226-2227
    • Seyedsayamdost, M.R.1    Stubbe, J.2
  • 16
    • 33644647904 scopus 로고    scopus 로고
    • 356 with 3,4-dihydroxyphenylalanine in the β2 subunit of E. coli ribonucleotide reductase
    • 356 with 3,4-dihydroxyphenylalanine in the β2 subunit of E. coli ribonucleotide reductase. J Am Chem Soc 128 (2006) 2522-2523
    • (2006) J Am Chem Soc , vol.128 , pp. 2522-2523
    • Seyedsayamdost, M.R.1    Stubbe, J.2
  • 17
    • 32244433011 scopus 로고    scopus 로고
    • 356 is a redox-active amino acid along the radical propagation pathway
    • This paper demonstrates the importance of Tyr356 as a hopping relay for ET through ribonucleotide reductase.
    • 356 is a redox-active amino acid along the radical propagation pathway. J Am Chem Soc 128 (2006) 1562-1568. This paper demonstrates the importance of Tyr356 as a hopping relay for ET through ribonucleotide reductase.
    • (2006) J Am Chem Soc , vol.128 , pp. 1562-1568
    • Seyedsayamdost, M.R.1    Yee, C.S.2    Reece, S.Y.3    Nocera, D.G.4    Stubbe, J.5
  • 18
    • 34447512997 scopus 로고    scopus 로고
    • Photoactive peptides for light-initiated tyrosyl radical generation and transport into ribonucleotide reductase
    • Reece S.Y., Seyedsayamdost M.R., Stubbe J., and Nocera D.G. Photoactive peptides for light-initiated tyrosyl radical generation and transport into ribonucleotide reductase. J Am Chem Soc 129 (2007) 8500-8509
    • (2007) J Am Chem Soc , vol.129 , pp. 8500-8509
    • Reece, S.Y.1    Seyedsayamdost, M.R.2    Stubbe, J.3    Nocera, D.G.4
  • 20
    • 53849136587 scopus 로고    scopus 로고
    • Development of a model system for the study of long distance electron transfer in peptides
    • Cordes M., Jacques O., Köttgen A., Jasper C., and Giese B. Development of a model system for the study of long distance electron transfer in peptides. Adv Synth Catal 350 (2008) 1053-1062
    • (2008) Adv Synth Catal , vol.350 , pp. 1053-1062
    • Cordes, M.1    Jacques, O.2    Köttgen, A.3    Jasper, C.4    Giese, B.5
  • 21
    • 43849113277 scopus 로고    scopus 로고
    • Influence of amino acid side chains on long-distance electron transfer in peptides: electron hopping via "stepping stones"
    • This paper describes the ability of aromatic amino acids to serve as stepping-stones for ET.
    • Cordes M., Köttgen A., Jasper C., Jacques O., Boudebous H., and Giese B. Influence of amino acid side chains on long-distance electron transfer in peptides: electron hopping via "stepping stones". Angew Chem Int Ed 47 (2008) 3461-3463. This paper describes the ability of aromatic amino acids to serve as stepping-stones for ET.
    • (2008) Angew Chem Int Ed , vol.47 , pp. 3461-3463
    • Cordes, M.1    Köttgen, A.2    Jasper, C.3    Jacques, O.4    Boudebous, H.5    Giese, B.6
  • 22
    • 46449093308 scopus 로고    scopus 로고
    • Rate measurements demonstrate the influence of tryptophan on long distance ET in azurin.
    • Shih C., Museth A.K., Abrahamsson M., Blanco-Rodriguez A.M., Di Bilio A.J., et al. Science 320 (2008) 1760-1762. Rate measurements demonstrate the influence of tryptophan on long distance ET in azurin.
    • (2008) Science , vol.320 , pp. 1760-1762
    • Shih, C.1    Museth, A.K.2    Abrahamsson, M.3    Blanco-Rodriguez, A.M.4    Di Bilio, A.J.5
  • 23
    • 0242500910 scopus 로고    scopus 로고
    • Anomalous distance dependence of electron transfer across peptide bridges
    • Antonello S., Formaggio F., Moretto A., Toniolo C., and Maran F. Anomalous distance dependence of electron transfer across peptide bridges. J Am Chem Soc 125 (2003) 2874-2875
    • (2003) J Am Chem Soc , vol.125 , pp. 2874-2875
    • Antonello, S.1    Formaggio, F.2    Moretto, A.3    Toniolo, C.4    Maran, F.5
  • 24
    • 12944302120 scopus 로고    scopus 로고
    • Evidence against the hopping mechanism as an important electron transfer pathway for conformationally constrained oligopeptides
    • Polo F., Antonello S., Formaggio F., Toniolo C., and Maran F. Evidence against the hopping mechanism as an important electron transfer pathway for conformationally constrained oligopeptides. J Am Chem Soc 127 (2005) 492-493
    • (2005) J Am Chem Soc , vol.127 , pp. 492-493
    • Polo, F.1    Antonello, S.2    Formaggio, F.3    Toniolo, C.4    Maran, F.5
  • 25
    • 84961983659 scopus 로고    scopus 로고
    • Dissociative electron transfer in donor-peptide-acceptor systems: results for kinetic parameters from a density functional/polarizable continuum model
    • Barone V., Newton M.D., and Improta R. Dissociative electron transfer in donor-peptide-acceptor systems: results for kinetic parameters from a density functional/polarizable continuum model. J Phys Chem B 110 (2006) 12632-12639
    • (2006) J Phys Chem B , vol.110 , pp. 12632-12639
    • Barone, V.1    Newton, M.D.2    Improta, R.3
  • 26
    • 33644782830 scopus 로고    scopus 로고
    • Theoretical study of long range electron transfer in phthalimide-peptide-methyl aminoacetate model molecules
    • Gao X., Zhou W., and Zhang W. Theoretical study of long range electron transfer in phthalimide-peptide-methyl aminoacetate model molecules. Chem Phys 322 (2006) 366-376
    • (2006) Chem Phys , vol.322 , pp. 366-376
    • Gao, X.1    Zhou, W.2    Zhang, W.3
  • 27
    • 34548398569 scopus 로고    scopus 로고
    • Long-range electron transfer across peptide chains with different secondary structures
    • Gao X., Tang S., and Zhou W. Long-range electron transfer across peptide chains with different secondary structures. Chem Phys Lett 445 (2007) 297-302
    • (2007) Chem Phys Lett , vol.445 , pp. 297-302
    • Gao, X.1    Tang, S.2    Zhou, W.3
  • 28
    • 0040122453 scopus 로고    scopus 로고
    • New mechanism for facile charge transport in polypeptides
    • Baranov L.Y., and Schlag E.W. New mechanism for facile charge transport in polypeptides. Z Naturforsch A 54 (1999) 387-396
    • (1999) Z Naturforsch A , vol.54 , pp. 387-396
    • Baranov, L.Y.1    Schlag, E.W.2
  • 29
    • 34250792228 scopus 로고    scopus 로고
    • Distal charge transport in peptides
    • This paper discusses the participation of amide groups in electron hopping processes.
    • Schlag E.W., Sheu S.-Y., Yang D.-Y., Selzle H.L., and Lin S.H. Distal charge transport in peptides. Angew Chem Int Ed 46 (2007) 3120-3196. This paper discusses the participation of amide groups in electron hopping processes.
    • (2007) Angew Chem Int Ed , vol.46 , pp. 3120-3196
    • Schlag, E.W.1    Sheu, S.-Y.2    Yang, D.-Y.3    Selzle, H.L.4    Lin, S.H.5
  • 30
    • 34248669849 scopus 로고    scopus 로고
    • Theoretical investigation on intramolecular electron transfer in polypeptides
    • Santhanamoorthi N., Kolandaivel P., and Senthilkumar K. Theoretical investigation on intramolecular electron transfer in polypeptides. Chem Phys Lett 440 (2007) 302-307
    • (2007) Chem Phys Lett , vol.440 , pp. 302-307
    • Santhanamoorthi, N.1    Kolandaivel, P.2    Senthilkumar, K.3
  • 31
    • 7444258599 scopus 로고    scopus 로고
    • Long-range electron transfer across peptide bridges: the transition from electron superexchange to hopping
    • Malak R.A., Gao Z., Wishart J.F., and Isied S.S. Long-range electron transfer across peptide bridges: the transition from electron superexchange to hopping. J Am Chem Soc 126 (2004) 13888-13889
    • (2004) J Am Chem Soc , vol.126 , pp. 13888-13889
    • Malak, R.A.1    Gao, Z.2    Wishart, J.F.3    Isied, S.S.4
  • 32
    • 84961983615 scopus 로고    scopus 로고
    • Conformational analysis of the electron-transfer kinetics across oligoproline peptides using N,N-dimethyl-1,4-benzenediamine donors and pyrene-1-sulfonyl acceptors
    • Issa J.B., Salameh A.S., Castner E.W., Wishart J.F., and Isied S.S. Conformational analysis of the electron-transfer kinetics across oligoproline peptides using N,N-dimethyl-1,4-benzenediamine donors and pyrene-1-sulfonyl acceptors. J Phys Chem B 111 (2007) 6878-6886
    • (2007) J Phys Chem B , vol.111 , pp. 6878-6886
    • Issa, J.B.1    Salameh, A.S.2    Castner, E.W.3    Wishart, J.F.4    Isied, S.S.5
  • 33
    • 34548213830 scopus 로고    scopus 로고
    • Orientation-dependent kinetics of heterogeneous electron transfer for cytochrome c immobilized on gold: electrochemical determination and theoretical prediction
    • Bortolotti C.A., Borsari M., Sola M., Chertkova R., Dolgikh D., Kotlyar A., and Facci P. Orientation-dependent kinetics of heterogeneous electron transfer for cytochrome c immobilized on gold: electrochemical determination and theoretical prediction. J Phys Chem C 111 (2007) 12100-12105
    • (2007) J Phys Chem C , vol.111 , pp. 12100-12105
    • Bortolotti, C.A.1    Borsari, M.2    Sola, M.3    Chertkova, R.4    Dolgikh, D.5    Kotlyar, A.6    Facci, P.7
  • 35
    • 18744363629 scopus 로고    scopus 로고
    • Electron transfer and catalytic control by the iron-sulfur clusters in a respiratory enzyme, E. coli fumarate reductase
    • Hudson J.M., Heffron K., Kotlyar V., Yelizateva S., Maklashina E., Cecchini G., and Armstrong F.A. Electron transfer and catalytic control by the iron-sulfur clusters in a respiratory enzyme, E. coli fumarate reductase. J Am Chem Soc 127 (2005) 6977-6989
    • (2005) J Am Chem Soc , vol.127 , pp. 6977-6989
    • Hudson, J.M.1    Heffron, K.2    Kotlyar, V.3    Yelizateva, S.4    Maklashina, E.5    Cecchini, G.6    Armstrong, F.A.7
  • 36
    • 30744452491 scopus 로고    scopus 로고
    • Electron flow in multicenter enzymes: theory, applications, and consequences on the natural design of redox chains
    • In this paper, protein film voltammetry is used to gain information about the design of cofactor redox chains.
    • Léger C., Lederer F., Guigliarelli B., and Bertrand P. Electron flow in multicenter enzymes: theory, applications, and consequences on the natural design of redox chains. J Am Chem Soc 128 (2006) 180-187. In this paper, protein film voltammetry is used to gain information about the design of cofactor redox chains.
    • (2006) J Am Chem Soc , vol.128 , pp. 180-187
    • Léger, C.1    Lederer, F.2    Guigliarelli, B.3    Bertrand, P.4
  • 37
    • 0038637051 scopus 로고    scopus 로고
    • Long-range electron transfer over 4 nm governed by an inelastic hopping mechanism in self-assembled monolayers of helical peptides
    • Morito T., and Kimura S. Long-range electron transfer over 4 nm governed by an inelastic hopping mechanism in self-assembled monolayers of helical peptides. J Am Chem Soc 125 (2003) 8732-8733
    • (2003) J Am Chem Soc , vol.125 , pp. 8732-8733
    • Morito, T.1    Kimura, S.2
  • 38
    • 39649105446 scopus 로고    scopus 로고
    • Distance dependence of long-range electron transfer through helical peptides
    • Kai M., Takeda K., Morita T., and Kimura S. Distance dependence of long-range electron transfer through helical peptides. J Pept Sci 14 (2008) 192-202
    • (2008) J Pept Sci , vol.14 , pp. 192-202
    • Kai, M.1    Takeda, K.2    Morita, T.3    Kimura, S.4
  • 40
    • 23844512824 scopus 로고    scopus 로고
    • Effects of dipole moment, linkers, and chromophores at side chains on long-range electron transfer through helical peptides
    • Watanabe J., Morita T., and Kimura S. Effects of dipole moment, linkers, and chromophores at side chains on long-range electron transfer through helical peptides. J Phys Chem B 109 (2005) 14416-14425
    • (2005) J Phys Chem B , vol.109 , pp. 14416-14425
    • Watanabe, J.1    Morita, T.2    Kimura, S.3
  • 41
    • 33745511427 scopus 로고    scopus 로고
    • Electron transfer across α-helical peptides: potential influence of molecular dynamics
    • Mandal H.S., and Kraatz H.-B. Electron transfer across α-helical peptides: potential influence of molecular dynamics. Chem Phys 326 (2006) 246-251
    • (2006) Chem Phys , vol.326 , pp. 246-251
    • Mandal, H.S.1    Kraatz, H.-B.2
  • 42
    • 40849126614 scopus 로고    scopus 로고
    • Photo-induced vectorial electron transfer through oriented metal-coordinated peptide assembly on a self-assembled monolayer
    • Higushi M. Photo-induced vectorial electron transfer through oriented metal-coordinated peptide assembly on a self-assembled monolayer. Thin Solid Films 516 (2008) 4312-4318
    • (2008) Thin Solid Films , vol.516 , pp. 4312-4318
    • Higushi, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.