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Volumn 121, Issue 41, 1999, Pages 9497-9502

Mechanisms of sulfoxidation catalyzed by high-valent intermediates of heme enzymes: Electron-transfer vs oxygen-transfer mechanism

Author keywords

[No Author keywords available]

Indexed keywords

HEME; HORSERADISH PEROXIDASE; MYOGLOBIN;

EID: 0032706535     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9901359     Document Type: Article
Times cited : (167)

References (37)
  • 26
    • 0033556669 scopus 로고    scopus 로고
    • Since Mb mutants we have prepared are able to catalyze olefin epoxidations while HRP cannot, we rather like to call the Mb mutant a P450 model in this report. Ozaki, S.; Yang, H.-J.; Matsui, T.; Goto, Y.; Watanabe Y. Tetrahedron: Asymmetry 1999, 10, 183-192.
    • (1999) Tetrahedron: Asymmetry , vol.10 , pp. 183-192
    • Ozaki, S.1    Yang, H.-J.2    Matsui, T.3    Goto, Y.4    Watanabe, Y.5
  • 30
    • 0345007360 scopus 로고    scopus 로고
    • note
    • Linear relationships were observed between the pseudo-first-order rate constants and the sulfide concentrations for the reactions with p-methylthioanisole and thioanisole. In the case of the reaction with p-methoxythioanisole, however, the pseudo-first-order rate constant exhibits a saturation behavior at the high concentrations. Thus the rate at [p-methoxythioanisole] = 125 μM was used for the determination of a bimolecular rate constant for this reaction.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.