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Volumn 125, Issue 43, 2003, Pages 13034-13035

Kinetic Evaluation of Phenolase Activity of Tyrosinase Using Simplified Catalytic Reaction System

Author keywords

[No Author keywords available]

Indexed keywords

2 QUINONE; CATECHOL; COPPER ION; HYDROXYLAMINE; META TYROSINE; MONOPHENOL MONOOXYGENASE; PHENOL DERIVATIVE; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0142214624     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja036425d     Document Type: Article
Times cited : (103)

References (32)
  • 11
    • 0037216767 scopus 로고    scopus 로고
    • For recent kinetic studies on the phenolase and catecholase activities, see: (a) Haghbeen, K.; Tan, E. W. Anal. Biochem. 2003, 312, 23-32.
    • (2003) Anal. Biochem. , vol.312 , pp. 23-32
    • Haghbeen, K.1    Tan, E.W.2
  • 17
    • 0036009142 scopus 로고    scopus 로고
    • For geometric discussions on each step in the catalytic mechanism, see: (a) Gerdemann, C.; Eicken, C.; Krebs, B. Acc. Chem. Res. 2002, 35, 183-191.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 183-191
    • Gerdemann, C.1    Eicken, C.2    Krebs, B.3
  • 25
    • 1542296467 scopus 로고    scopus 로고
    • Que, L., Jr., Tolman, W. B., Eds; Elsevier: Oxford. In press
    • Itoh, S. In Comprehensive Coordination Chemistry-11; Que, L., Jr., Tolman, W. B., Eds; Elsevier: Oxford, 2003. In press.
    • (2003) Comprehensive Coordination Chemistry-11
    • Itoh, S.1
  • 26
    • 0142181662 scopus 로고    scopus 로고
    • note
    • When hydrogen peroxide was added into a solution of met-tyrosinase, the absorption band at 345 nm due to oxy-tyrosinase was generated (Figure S1). However, the absorption band readily disappeared when the solution was degassed. Thus, we could not perform single-turnover kinetic analysis on the reaction between oxy-tyrosinase and phenols.
  • 29
    • 0142150690 scopus 로고    scopus 로고
    • note
    • 2OH. It is, however, apparent that the enzymatic over oxidation of catechols to the quinones is not involved, since the catechol oxidation does not proceed at all in the present borate buffer system.
  • 30
    • 0142150689 scopus 로고    scopus 로고
    • note
    • The detailed kinetic analysis is presented in Supporting Information (S3).
  • 32
    • 0041732439 scopus 로고    scopus 로고
    • Rate-dependence on the oxidation potentials of phenols in the present enzymatic reaction is totally different from that observed in the oxidation reaction of neutral phenols (phenoxyl radical formation) by the peroxo complex which proceeds via a proton-coupled electron transfer (PCET) mechanism: Osako, T.; Ohkubo, K.; Taki, M.; Tachi, Y.; Fukuzumi, S.; Itoh, S. J. Am. Chem. Soc. 2003, 125, 11027-11033.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11027-11033
    • Osako, T.1    Ohkubo, K.2    Taki, M.3    Tachi, Y.4    Fukuzumi, S.5    Itoh, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.