Premium
Kinetic effects of multiple charge modifications in enzyme‐substrate reactions: Brownian dynamics simulations of Cu, Zn superoxide dismutase
Author(s) -
Sines Jacqueline J.,
McCammon J. Andrew,
Allison Stuart A.
Publication year - 1992
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.540130108
Subject(s) - chemistry , enzyme , kinetics , brownian dynamics , substrate (aquarium) , superoxide dismutase , diffusion , brownian motion , enzyme kinetics , reaction rate constant , kinetic energy , active site , biochemistry , thermodynamics , physics , quantum mechanics , oceanography , geology
We used Brownian dynamics simulations of substrate O 2 −encounters with the enzyme bovine erythrocyte Cu, Zn superoxide dismutase (SOD) to study the effects of multiple charge modifications in the enzyme on the kinetics of its diffusion‐controlled reaction. When the charges of two or three residues were changed, the calculated rate consant relative to that for the unmodified enzyme was usually found to be the product of relative rate constants for the enzymes with the corresponding single‐site changes. This “multiplicativity” rule may be useful in the design of enzymes that operate with diffusion‐controlled kinetics. Residues that deviate from the general rule are found in the active site channel of SOD, and the origin of these deviations is considered.