Rhodospirillum rubrum heme protein

Aono, S., Nakajima, H., Saito, K., and Okada, M., 1996, A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum, Biochem. Biophys. Res. Commun. 228(3) 752n756. 

Shelver, D., Kerby, R. L., He, Y. P., and Roberts, G. P., 1997, CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein, Proc. Natl. Acad. Sci. USA 94(21) 11216nll220. 

Many cytochromes in energy-transducing organelles are membrane-bound proteins. Present in mitochondria and in purple photosynthetic bacteria, the cyt bc complex (also called ubiquinol-cytochrome c oxidoreductase, or complex III) catalyzes the electron transfer from ubiquinol to ferricyt c and pumps protons from the matrix to the cytosol.The catalytic core of the cyt bci complex comprises three redox-active subunits they are a cyt b with two ft-type hemes bn and bf), a cyt Cl, and a Reiske iron sulfur protein. While this catalytic core has enzymatic activity in some a proteobacteria like Paracoccus, Rhodospirillum rubrum, and Rb. capsulatus, mitochondrial cyt bci complexes have an additional seven or eight subunits." ... 

Cytochrome c from Rhodospirillum rubrum consists of a dimer (mol. wt. 27,500) with identical subunits, each containing a heme prosthetic group (Meyer et a/., 1975). At neutral pH the ESR spectra of the oxidized protein consists of signals with g values close to 5, atypical of either low-spin or high-spin ferric hemes. This observation has been rationalized in terms of... 

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