Abstract
Picosecond CO recombination kinetics have been measured after photodissociation of the artificial complexes calmodulin ∗ heme-CO and calmodulin ∗ heme-CO ∗ melittin. These systems show an enhancement of the geminate fraction of kinetics relative to unbound heme-CO, due in part to fast geminate kinetics (τ = 50 ps for the initial phase), as well as a decrease in the rate of migration of CO away from the binding site. This indicates that calmodulin provides a complete pocket around the heme group. Rather than competing with the hemes for binding to calmodulin, the melittin seems to act as a cap to further enclose the hemes; melittin increases the affinity of calmodulin for heme-CO, but only weakly affects the CO recombination kinetics.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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