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Volumn 108, Issue 43, 2004, Pages 16912-16917

Probing electron tunneling pathways: Electrochemical study of rat heart cytochrome c and its mutant on pyridine-terminated SAMs

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROMES; ELECTRON-TRANSFER RATES; MOLECULAR STATES; TUNNELING PATHWAY;

EID: 8344271158     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp048148i     Document Type: Article
Times cited : (66)

References (42)
  • 24
    • 0037077659 scopus 로고    scopus 로고
    • The primary evidence for the direct ligation between the pyridine and the heme unit is the negative shift in redox potential and the Raman spectra for the adsorbed protein. See (a) Wei, J.; Liu, H.; Dick, A.; Yamamoto, H.; He, Y.; Waldeck, D. H. J. Am. Chem. Soc. 2002, 124, 9591.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9591
    • Wei, J.1    Liu, H.2    Dick, A.3    Yamamoto, H.4    He, Y.5    Waldeck, D.H.6
  • 31
    • 0001318962 scopus 로고    scopus 로고
    • Bard, A. J., Rubinstein, I., Eds.; Marcel Dekker: New York
    • (a) Finklea, H. O. In Electroanalytical Chemistry; Bard, A. J., Rubinstein, I., Eds.; Marcel Dekker: New York, 1996; Vol. 19, p 109.
    • (1996) Electroanalytical Chemistry , vol.19 , pp. 109
    • Finklea, H.O.1
  • 38
    • 8344264214 scopus 로고    scopus 로고
    • note
    • Attempts to adsorb the protein onto thinner films gave a faradaic response, but the apparent redox potential of the protein was shifted considerably from the other data. Because those results are suspect, they are not included. Attempts to study thicker films were not fruitful because the signal is too weak.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.