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Volumn 129, Issue 43, 2007, Pages 13118-13126

Spectroscopic and kinetic studies of perturbed trinuclear copper clusters: The role of protons in reductive cleavage of the O-O bond in the multicopper oxidase Fet3p

Author keywords

[No Author keywords available]

Indexed keywords

COORDINATION REACTIONS; PEROXIDES; PERTURBATION TECHNIQUES; PROTON TRANSFER; REACTION KINETICS;

EID: 35848952080     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja073905m     Document Type: Article
Times cited : (57)

References (49)
  • 42
    • 35848933348 scopus 로고    scopus 로고
    • In the spectra shown in Figure 3, ε ≈ 3000 M-1 cm -1 for the 330 nm band because the spectrum of the reduced protein has been subtracted to eliminate the contribution of the protein 280 nm band. In the presence of the 280 nm band the ε ≈ 5000 M-1 cm -1 for the 330 nm band
    • -1 for the 330 nm band.
  • 45
    • 0004234130 scopus 로고
    • 6th ed, Allyn and Bacon: Newton, MA
    • Morrison, R. T.; Boyd, R. N. Organic Chemistry, 6th ed.; Allyn and Bacon: Newton, MA, 1987; pp 849-851.
    • (1987) Organic Chemistry , pp. 849-851
    • Morrison, R.T.1    Boyd, R.N.2
  • 49
    • 35848938389 scopus 로고    scopus 로고
    • - where in the holoenzyme an electron from the reduced T1 Cu in the PI has been transferred to the TNC and the O-O bond is ready to undergo a two-electron reductive cleavage.
    • - where in the holoenzyme an electron from the reduced T1 Cu in the PI has been transferred to the TNC and the O-O bond is ready to undergo a two-electron reductive cleavage.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.