A membrane‐bound HIPIP type center in the thermohalophile Rhodothermus marinus

A HIPIP-type center was discovered in intact membranes of the thermohalophilic aerobe Rhodothermus marinus. In both the membrane-bound state and after detergent solubilization and partial purification, this center exhibits an almost axial EPR spectrum, with g-values at 2.13 and 2.03, similar to those of soluble HIPIP proteins isolated from purple bacteria. It has a high reduction potential, of 260 mV at pH 7.5. Rhodothermus HIPIP is involved in the main membrane-bound electron-transfer pathway, being reduced by NADH or succinate only in the presence of cyanide. The possible physiological function of this novel HIPIP-type center is discussed.