Abstract
Cytochromecd 1 nitrite reductase is a bifunctional multiheme enzyme catalyzing the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of dioxygen to water. Kinetics and thermodynamics of the internal electron transfer process in thePseudomonas stutzeri enzyme have been studied and found to be dominated by pronounced interactions between thec- and thed 1- hemes. The interactions are expressed in both dramatic changes in the internal electron transfer rates between these sites and in marked cooperativity in their electron affinity. The results constitute a prime example of intra-protein control of the electron transfer rates by allosteric interactions.
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