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Volumn 125, Issue 13, 2003, Pages 3722-3732

Distance dependence of electron transfer across peptides with different secondary structures: The role of peptide energetics and electronic coupling

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CHARGE TRANSFER; CONFORMATIONS; MAGNETIC MOMENTS; MOLECULAR STRUCTURE; PROTEINS; REACTION KINETICS;

EID: 0242500928     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja020358q     Document Type: Article
Times cited : (149)

References (84)
  • 37
    • 0242528006 scopus 로고    scopus 로고
    • Hush, N. S. 1967; Vol. 8, p 391
    • Hush, N. S. 1967; Vol. 8, p 391.
  • 44
    • 0242444503 scopus 로고    scopus 로고
    • note
    • DA only if the interested transition is found within the lowest 150 transition.
  • 50
    • 0242444502 scopus 로고    scopus 로고
    • note
    • When the D and A groups are placed around the α-helix, the physical separation between D and A does not increase linearly with n.
  • 51
    • 0242528005 scopus 로고    scopus 로고
    • note
    • 3n- groups was also observed similar to that in the β-strand and polyproline II secondary structures.
  • 52
    • 0242696865 scopus 로고    scopus 로고
    • note
    • 3n- bridge can only be due to the Coulombic effects since no carbonyl groups are present in the hydrocarbon bridges to give rise to additional ground-state dipoles.
  • 55
    • 0242527994 scopus 로고    scopus 로고
    • note
    • -1). This is expected because of the small perturbation introduced by the metal ions. However, it should be mentioned that if the orbital energies of donor and acceptor are in the proximity of the peptide π- and π*-orbitals, β-values will change. Such systems are not the subject of this work. Effect of specific hydration on β-values was carried out using the method described in ref 58 where specific water molecules around metal ions were introduced. The results here again show no significant change on the β-values. More extensive calculations involving solvents as a continuum are underway and may lead to a further refinement of these conclusions.
  • 75
    • 0242612755 scopus 로고    scopus 로고
    • note
    • The driving force for the reaction is reported to be ∼0.4 V, and the reorganization energy is also reported as ∼1.2 V (using the two-sphere model). Thus, these reactions occur in the normal Marcus regime. For our calculations, the reorganization energy was not needed. We estimated the perturbation of molecular orbital energy at the D and A sites (ΔΔE) due to the point dipole generated by C=O groups. For the six-peptide bridge in the α-helical structure comparable to the compound used in Galoppini's experiment, ΔΔE was 24.4 kK in a vacuum or 0.082 V in acetonitrile. From this value, the ratio for the electron transfer in the direction of the molecular dipole vs that against the molecular dipole can be calculated using the equation k(f)/k(r) = exp(-ΔΔE/2RT). Note that if the reaction is activationless, directional dependence will be very small and hard to detect
  • 76
    • 0003601534 scopus 로고
    • Merck & Co.: Rahway, NJ
    • The Merck Index, 11th ed; Merck & Co.: Rahway, NJ, 1989, p 63.
    • (1989) The Merck Index, 11th Ed. , pp. 63


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.