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From a careful steady-state kinetic study it is shown that the inhibition of L-lactate oxidation by cytochrome b2 with ferricyanide as acceptor is of the mixed competitive-noncompetitive type, indicating the formation of an active ternary complex between enzyme, substrate, and inhibitor. With a large excess of acceptor, the simplest formal mechanism(More)
The temperature jump relaxation technique is a convenient and general means of studying rapid reversible reactions of biological macromolecules. Recent advances in automatic data acquisition and the introduction of different optical detection systems will soon allow us to exploit the full potential of kinetic measurements near equilibrium. On the other(More)
Oxalate is the strongest known inhibitor of yeast cytochrome b2 activity. We have used spectrophotometric titration, temperature-jump relaxation, and calorimetry in an investigation of the interaction between enzyme and inhibitor. The titration data are consistent with noncooperative binding to one site per subunit. This conclusion is corroborated by(More)
The calculation of chemical relaxation amplitudes for a reaction mechanism involving an arbitrary number of thermodynamically independent steps is discussed. A formalism is developed which considerably reduces the computational labor required to derive expressions relating experimental amplitudes to thermodynamic functions and specific signal changes of(More)