The reaction center associated tetraheme cytochrome subunit from Chromatium vinosum revisited: a reexamination of its EPR properties.

The heme components of chromatophore membranes from the purple bacterium Chromatium vinosum have been studied by EPR. Five different heme species could be distinguished on the basis of their g values, redox midpoint potentials, and orientations of heme planes with respect to the membrane plane: gz = 2.94, Em = +10 mV, 40 degrees-50 degrees; gz = 2.94, Em = +10 mV, 0 degree; gz = 3.1, Em = +330 mV, 90 degrees; gz = 3.3, Em = 360 mV, 30 degrees; gz = 3.4, Em = 0 mV, no detectable orientation. Four of these five hemes (gz = 3.3, gz = 3.1, and 2x gz = 2.94) were ascribed to the tetraheme cytochrome subunit associated with the photosynthetic reaction center of this bacterium. Some of the results obtained have already been reported previously [Tiede, D.M., Leigh, J.S., & Dutton, P.L. (1978) Biochim. Biophys. Acta 503, 524-544] and have led to a model for the tetraheme cytochrome subunit in Chromatium which is significantly different from the three-dimensional structure of the reaction center associated subunit in the purple bacterium Rhodopseudomonas viridis. The additional data obtained in our work, however, require a reinterpretation of the previously published results. The model arrived at is in general agreement with the X-ray structure from Rhodopseudomonas viridis. A model rationalizing the detailed differences between the structure of the Rhodopseudomonas viridis cytochrome subunit and the data obtained on tetraheme subunits from other photosynthetic bacteria is presented.