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The Kinetic Mechanism(s) of Cytochrome Oxidase
Author(s) -
MYERS DAVID,
PALMER GRAHAM
Publication year - 1988
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1988.tb35325.x
Subject(s) - mechanism (biology) , cytochrome c oxidase , chemistry , kinetics , steady state (chemistry) , reaction mechanism , cytochrome , oxidase test , reaction rate constant , thermodynamics , enzyme , catalysis , biochemistry , physics , quantum mechanics
The steady-state kinetics of cytochrome oxidase exhibit two characteristics that impose severe constraints on any proposed mechanism. The first is the exponential consumption of ferrocytochrome c and the second is the nonhyperbolic dependence of reaction velocity upon the concentration of cytochrome c. Because the reaction mechanism contains at least five, and possibly six, substrates, realistic mechanisms can be very complex and not suitable for analysis by conventional means. We have developed procedures for rapidly establishing whether a postulated mechanism will exhibit the necessary behavior and for calculating the steady-state activity that will result for any mechanism, given values for the individual rate constants and reactant concentrations. The procedures have been used with mechanisms containing up to 40 enzyme species.