Single-turnover kinetics

Johnson and Fierke Hammes have presented detailed accounts of how rapid reaction techniques allow one to analyze enzymic catalysis in terms of pre-steady-state events, single-turnover kinetics, substrate channeling, internal equilibria, and kinetic partitioning. See Chemical Kinetics Stopped-Flow Techniques... 

Wong, I., Patel, S. S., and Johnson, K. A. (1991). An induced-fit kinetic mechanism for DNA replication fidelity Direct measurement by single-turnover kinetics. Biochemistry 30, 526-537. 

M. D. Wolfe, D. J. Altier, A. Stubna, C. V. Popescu, E. Miinck, J. D. Lipscomb, Benzoate 1, 2-dioxygenase from Pseudomonas putida Single turnover kinetics and regulation of a two-component Rieske dioxygenase. Biochemistry 41 (2002) 9611. 

Undsley, J.E. and Fuchs, R.P. (1994) Use of single-turnover kinetics to study bulky adduct bypass by T7 DNA polymerase. Biochemistry, 33, 764—772. 

Fio. 9. EPSP synthase single-turnover kinetics and EPSP synthase reaction pathway. (A) The disappearance and formation of PEP ( ), EPSP ( ), and intermediate (A) were monitored in the reverse direction. The reaction was initiated by mixing enzyme (10 /xM) and S3P (100 fiM) with radiolabeled PEP (3.5 /xAf). (B) The disappearance and formation of EPSP ( ), PEP ( ), and intermediate (A) were monitored in the reverse direction. The reaction was initiated by mixing enzyme (10 iiM) with phosphate (7.5 /zM) and radiolabeled EPSP (2.1 fiM). The curves were calculated by computer simulation using the fill kinetic pathway shown in Scheme XIX and the 12 individual rate constants (3). Reproduced with permission from (3). 

Single-turnover kinetic experiments provided evidence for a transient species with an absorption maximum at 312 nm. The intensity of that transient was increased by a S41A mutation. Rapid quenching of reaction... 

Single-turnover kinetic analysis revealed a transient with similar absorption as that of Compound Q, the pentacyclic intermediate of eubacterial riboflavin synthase (Figure 19). ... 

Brewer, C.B. and J.A. Peterson (1988) Single turnover kinetics of the reaction between oxycy-tochrome P450cam and reduced putidaredoxin. J. Biol. Chem. 263, 791-798. 

Rate constants are from the hest fit of single-turnover kinetics data to the reaction mechanism described by Scheme 6.1. The kinetic parameters are for the incorporation of dATP (correct nucleotide) on 13/ 20(T) priraer/template at pH 7.4 (50 mM Tris-Cl) and 21°C (53,54). 

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