Hepatic sulfite oxidase. Identification of the molybdenum center as the site of irreversible inactivation by ferricyanide

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Abstract

Ferricyanide, an artificial electron acceptor for hepatic sulfite oxidase (EC 1.8.3.1), has been shown to cause an irreversible inactivation of the enzyme by an interaction at the molybdenum center. The one-electron transferring abilities are lost first, followed by slower parallel losses of oxidase activity and enzymic molybdenum. The rate of inactivation by ferricyanide is lower in the presence of cytochrome c or any of several anions. Accompanying the loss of one-electron transfer activities are changes in the Mo(V) electron paramagnetic resonance signal and in the visible absorption spectrum. Specific degradation of the polypeptide chain takes place subsequently, but at a much slower rate than the inactivation. These results are discussed in relation to the pathways of electron entry, transport and egress in sulfite oxidase. © 1974.

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Kessler, D. L., & Rajagopalan, K. V. (1974). Hepatic sulfite oxidase. Identification of the molybdenum center as the site of irreversible inactivation by ferricyanide. BBA - Enzymology, 370(2), 399–409. https://doi.org/10.1016/0005-2744(74)90101-6

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