Myoglobin stopped-flow kinetics

The kinetics of myoglobin oxidation and reduction have been studied by a variety of experimental techniques that include stopped-flow kinetics, pulse radiolysis, and flash photolysis. In considering this work, attention is directed first at studies of the wild-type protein and then at experiments involving variants of Mb. 

The vast majority of fast ligand substitutions studied to date are in the s, ms, and fjLS time scales, which encompass a vast range of reactions, and for which fast reaction techniques have become both refined and readily commercially available. Not surprisingly the majority of reactions reported in this chapter fall into these time scales, and have been studied predominantly by stopped-flow, temperature-jump, or nuclear magnetic resonance fast reaction techniques, which are referred to by the initials SF, TJ, and NMR hereafter. However, substantial rewards await those who venture into the ns and ps time scale as shown by a study of the recombination kinetics of small ligands at the Fe(II) center of sperm whale and elephant myoglobins in which laser pulses of 1 ps and 4 ns facilitated the determination of rate constants in the range 3 x 10 to 5 x s and 10 to 10 ... 

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