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Volumn 105, Issue 33, 2001, Pages 7887-7907

Energetics and dynamics of enzymatic reactions

Author keywords

[No Author keywords available]

Indexed keywords

VIBRATIONALLY ENHANCED TUNNELING;

EID: 0035940264     PISSN: 10895647     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp011048h     Document Type: Review
Times cited : (308)

References (169)
  • 6
    • 0002676574 scopus 로고    scopus 로고
    • Wilson, E.K. C & EN 2000, 78 (29), 42-45.
    • (2000) C & EN , vol.78 , Issue.29 , pp. 42-45
    • Wilson, E.K.1
  • 15
    • 0011391799 scopus 로고    scopus 로고
    • note
    • The fact that the transmission factor depends on the number of times the trajectory moves back and forth on the transition state was questioned in ref 157. However, this recrossing effect is an integral part of current reaction rate formulations (e.g., refs 9 and 13). Reference 157 also questioned the fact that ref 10 verified the validity of the linear response approximation of eq 20 by averaging downhill trajectories, suggesting that no such calculation was reported in ref 10. Unfortunately, the author overlooked Figure 15 of ref 10.
  • 38
    • 0011443170 scopus 로고    scopus 로고
    • note
    • Kollman and co-workers called this approach QM-FE. However, since the QM calculations are done in the gas phase, we believe that such a name should be preserved to true coupled QM/MM-FEP approaches.
  • 41
    • 0011484248 scopus 로고    scopus 로고
    • note
    • The fact that the EVB surface is frequently recalibrated using theoretical and experimental information about the reference reaction in solution is an advantage rather than a disadvantage if reliable information about the reaction in the enzyme is desired. This is because the enzyme and solution surfaces are much more similar than the gas-phase and the solution surfaces. Not using information about solution reactions is similar to attempts to refine solvation models using only gas-phase calculations rather than solvation energies.
  • 87
    • 0011390215 scopus 로고    scopus 로고
    • note
    • 85 without a valid ground (see discussion in footnote 56 of ref 69) can be used to explore the origin of the catalytic effect of enzyme active sites.
  • 101
    • 0017251977 scopus 로고
    • Warshel, A. Nature 1976, 260, 679-683.
    • (1976) Nature , vol.260 , pp. 679-683
    • Warshel, A.1
  • 104
    • 0041912615 scopus 로고    scopus 로고
    • Energetics and dynamics of transition states of reactions in enzymes and solutions
    • Transition State Modeling for Catalysis; Truhlar, D., Morokuma, K., Eds.; American Chemical Socidty: Washington, DC
    • Warshel; A.; Bentzien, J. Energetics and Dynamics of Transition States of Reactions in Enzymes and Solutions. In Transition State Modeling for Catalysis; Truhlar, D., Morokuma, K., Eds.; ACS Sympsium Series 721; American Chemical Socidty: Washington, DC, 1999.
    • (1999) ACS Sympsium Series , vol.721
    • Warshel1    , A.2    Bentzien, J.3
  • 157
    • 85034146237 scopus 로고    scopus 로고
    • Proteins reactions and conformational change. Simple, complex, or both?
    • Frauenfelder, H., Deisenhofer, H., Wolynes, P.G., Eds.; Dahlem University Press: Berlin
    • Karplus, M. Proteins Reactions and Conformational Change. Simple, Complex, or Both? In Dahlem Workshop on Simplicity and Complexity in Proteins and Nucleic Acids; Frauenfelder, H., Deisenhofer, H., Wolynes, P.G., Eds.; Dahlem University Press: Berlin, 1999.
    • (1999) Dahlem Workshop on Simplicity and Complexity in Proteins and Nucleic Acids
    • Karplus, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.