Myoglobin oxidation 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. 

George and Stratmann (37) investigating the kinetics of the oxidation of myoglobin to metmyoglobin by molecular oxygen, under the same... 

Keywords HNO NO Nitroxyl Azanone Nitroxyl anion Nitrosyl Porphyrin Heme Iron Manganese Ruthenium Cobalt Reductive nitrosylation Kinetics Oxidation Protein Myoglobin NOS. 

An approach which has proved successful has been to introduce substituents into the porphyrin ring in such a manner that there is a steric hindrance to dimerization. Both picket fence and capped complexes have been identified. In the former example a model system is provided for the active site of both myoglobin and oxymyoglobin. The lifetime of the dioxygen complex of the latter type (1) is 20 h, at which time some iron(m) is present. Rapid auto-oxidation occurs in solution unless a strongly co-ordinating base (L) is present. Kinetic studies of this reaction are consistent with... 

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