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Volumn 107, Issue 22, 2003, Pages 5300-5305

The proximal hydrogen-bonded residue controls the stability of the compound II intermediate of peroxidases and catalases

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; CRYSTAL STRUCTURE; DISSOCIATION; HYDROGEN BONDS; PROBABILITY DENSITY FUNCTION;

EID: 0038171518     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp0268516     Document Type: Article
Times cited : (30)

References (48)
  • 2
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    • Enzymology and structure of catalases
    • Sykes, A. G., Mauk, G., Eds.; Academic Press: New York
    • (b) Nichols, P.; Fita, I.; Loewen, P. C. Enzymology and Structure of Catalases. In Advances in Inorganic Chemistry; Sykes, A. G., Mauk, G., Eds.; Academic Press: New York, 2001; Vol. 51, pp 51-106.
    • (2001) Advances in Inorganic Chemistry , vol.51 , pp. 51-106
    • Nichols, P.1    Fita, I.2    Loewen, P.C.3
  • 4
    • 0001480426 scopus 로고    scopus 로고
    • Horseradish peroxidase
    • Sykes, A. G., Mauk, G., Eds.; Academic Press: New York
    • (d) Veitch, G.; Smith, A. T. Horseradish Peroxidase. In Advances in Inorganic Chemistry; Sykes, A. G., Mauk, G., Eds.; Academic Press: New York, 2001; Vol. 51, pp 107-162
    • (2001) Advances in Inorganic Chemistry , vol.51 , pp. 107-162
    • Veitch, G.1    Smith, A.T.2
  • 26
    • 0038698950 scopus 로고    scopus 로고
    • Mutter, J. Max-Planck-Institut für Festkörperforschung: Stuttgart
    • (a) Computations were performed using the CPMD 3.0h program. Mutter, J. Max-Planck-Institut für Festkörperforschung: Stuttgart, 1998.
    • (1998) Computations were Performed Using the CPMD 3.0h Program
  • 29
    • 33744765040 scopus 로고    scopus 로고
    • For recent reviews on the applications of Car - Parrinello molecular dynamics to biology, In press
    • For recent reviews on the applications of Car - Parrinello molecular dynamics to biology, see: (a) Carloni, P.; Röthlisberger, U.; Parrinello, M. Ace. Chem. Res. In press
    • Ace. Chem. Res.
    • Carloni, P.1    Röthlisberger, U.2    Parrinello, M.3
  • 30
    • 0035785737 scopus 로고    scopus 로고
    • Simulations of enzymatic systems: Perspectives from Car-Parrinello molecular dynamics simulations
    • L. Eriksson. L., Ed.; Elsevier Science: New York
    • (b) Carloni, P.; Röthlisberger, U. Simulations of Enzymatic Systems: Perspectives from Car-Parrinello Molecular Dynamics Simulations. In Theoretical Biochemistry-Processes and Properties of Biological Systems; L. Eriksson. L., Ed.; Elsevier Science: New York, 2001; p 215.
    • (2001) Theoretical Biochemistry-Processes and Properties of Biological Systems , pp. 215
    • Carloni, P.1    Röthlisberger, U.2
  • 39
    • 0038698952 scopus 로고    scopus 로고
    • note
    • An investigation of the properties of putative OH-based compound II is in progress and the results will be published elsewhere.
  • 41
    • 0038698951 scopus 로고    scopus 로고
    • note
    • We do not observe tilting of the phenolate ligand with respect to the perpendicular to the porphyrin plane when viewing it along the perpendicular direction to the benzene ring. Probably the differences in electronic state between compound I (ref 11) and compound II (this work) are responsible for this variation.
  • 42
    • 0038360688 scopus 로고    scopus 로고
    • note
    • ε coordinate would be an interesting exercise to illustrate the influence of the excited-state structure on the dynamics of the system. However, this is out of the scope of the present study.
  • 48
    • 0038360691 scopus 로고    scopus 로고
    • An investigation of the catalytic reaction path using QM/MM methods is in progress
    • An investigation of the catalytic reaction path using QM/MM methods is in progress.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.