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Volumn 303, Issue 5, 2000, Pages 813-830

How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways

Author keywords

Buried active site; Cytochrome P450; Enzyme substrate binding; Molecular dynamics simulation; Protein dynamics

Indexed keywords

CAMPHOR 5 MONOOXYGENASE;

EID: 0034634391     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4155     Document Type: Article
Times cited : (151)

References (39)
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    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 23
    • 0034634393 scopus 로고    scopus 로고
    • How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms
    • (2000) J. Mol. Biol. , vol.303 , pp. 797-811
    • Ludemann, S.K.1    Lounnas, V.2    Wade, R.C.3
  • 24
    • 0003631066 scopus 로고
    • Cytochrome P450: Structure, mechanism and biochemistry
    • Twenty-five Years of P450cam Research: Mechanistic Insights into Oxygenase Catalysis (Ortiz de Montellano, P. R., ed.), Plenum Press, New York and London
    • (1995)
    • Mueller, E.J.1    Loida, P.J.2    Sligar, S.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.