Ferricyanide-mediated oxidation of ferrous oxygenated and carbonylated myoglobin (Mb(II)-O(2) and Mb(II)-CO, respectively) is limited by O(2) and CO dissociation, respectively, then the transient deoxygenated derivative (Mb(II)) is rapidly oxidized. Here, kinetics of ferricyanide-mediated oxidation of ferrous nitrosylated sperm whale myoblobin (Mb(II)-NO) is reported. Unlike for Mb(II)-O(2) and Mb(II)-CO, ferricyanide reacts with Mb(II)-NO forming first a transient ferric nitrosylated species (Mb(III)-NO), followed by the ()NO dissociation from Mb(III)-NO. Values of the second-order rate constant for ferricyanide-mediated oxidation of Mb(II)-NO (i.e., for the formation of the transient Mb(III)-NO species) and of the first-order rate constant for ()NO dissociation from Mb(III)-NO (i.e., for Mb(III) formation) are (1.3+/-0.2)x10(6)M(-1)s(-1) and 7.6+/-1.3s(-1), respectively, at pH 8.3 and 20.0 degrees C. Since ()NO dissociation from Mb(II)-NO is very slow, and (unlike O(2) and CO) ()NO is a ligand for both Mb(II) and Mb(III), Mb(II)-NO can be oxidized without requiring ()NO dissociation.