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Volumn 126, Issue 38, 2004, Pages 11814-11819

Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer?

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; ELECTRON TRANSITIONS; ELECTROSTATICS; FREE ENERGY; HYDROLYSIS; NEGATIVE IONS;

EID: 4644314829     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0480421     Document Type: Article
Times cited : (46)

References (57)
  • 11
    • 0000174890 scopus 로고    scopus 로고
    • Sinnott, M. L., Ed.; Academic Press: London
    • (b) Hengge, A. C. In Comprehensive Biological Catalysis; Sinnott, M. L., Ed.; Academic Press: London, 1998; Vol. 1, pp 517-542.
    • (1998) Comprehensive Biological Catalysis , vol.1 , pp. 517-542
    • Hengge, A.C.1
  • 38
    • 4644368743 scopus 로고    scopus 로고
    • note
    • (e) The nonenzymatic hydrolysis of para-nitrophenyl phosphate and para-nitrophenyl sulfate was found to occur via P-O and S-O bond cleavage, respectively (ref 9a and c).
  • 48
    • 4644330910 scopus 로고    scopus 로고
    • note
    • a values of this order for the incoming and leaving groups do not lead to large transition-state asymmetries (refs 17 and 18).
  • 55
    • 0013191081 scopus 로고
    • Eichhorn, G. L., Ed.; Elsevier: Amsterdam
    • (a) Spiro, T. G. In Inorganic Biochemistry; Eichhorn, G. L., Ed.; Elsevier: Amsterdam, 1973; Vol. 1, pp 549-581.
    • (1973) Inorganic Biochemistry , vol.1 , pp. 549-581
    • Spiro, T.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.