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. 1995 Nov 20;375(3):197-200.
doi: 10.1016/0014-5793(95)01188-k.

HiPiP oxido-reductase activity in membranes from aerobically grown cells of the facultative phototroph Rhodoferax fermentans

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HiPiP oxido-reductase activity in membranes from aerobically grown cells of the facultative phototroph Rhodoferax fermentans

A Hochkoeppler et al. FEBS Lett. .
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Abstract

The role of the periplasmically located, water-soluble, HiPIP (high-potential iron-sulfur protein) in the respiratory chain of the facultative phototroph Rhodoferax fermentans has been examined. The oxidized HiPIP is reduced by succinate-dependent respiration via the bc1 complex, this reaction being inhibited by myxothiazol and/or stigmatellin. The reduced HiPIP can be oxidized by the membrane-bound cytochrome oxidase, this reaction being inhibited by 0.1 mM cyanide. We conclude that aerobically grown Rf. fermentans contains a redox chain in which HiPIP mediates electron transfer between the bc1 complex and the cb-type cytochrome oxidase.

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