Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1.

Conversion of spin state and protein structure in Rhodospirillum rubrum ferric cytochrome c' coupled with dissociation of dimer

“…The aromatic protons are distributed in a range wider than those of simple proteins presumably due to the effect of the ring current and the paramagnetic center of the heme group. The monomer of the protein contains three tyrosine, four phenylalanine, two histidine, and one tryptophan residues (Meyer et al, 1975).…”

“…Molecular Weight of Cytochrome c' in Each Spin State. The molecular weight of the monomer subunit of R. rubrum cytochrome c'is known to be 14000 on the basis of the amino acid sequence (Meyer et al, 1975). The apparent molecular weight of the cytochrome c' under different conditions was measured by the sedimentation equilibrium method to see if there was any form other than the dimer form.…”

“…The single subunit is composed of 126 amino acids (Mr 14000), and its sequence was determined (Meyer et al, 1975).…”

Nuclear magnetic resonance studies of Rhodospirillum rubrum cytochrome c'

“…These proteins are placed in the cytochrome c' class of heme proteins by virtue of their possession of a heme group covalently bound to the protein via thioether linkages and the high-spin nature of the heme iron. The sequence of nine cytochromes c'have been determined, and all possess heme binding units (Cys-x-y-Cys-His)* 1 located near the C-terminus (Ambler, 1973;Meyer et al, 1975;Ambler et al, 1979a,b; R. P. Ambler, unpublished data). By analogy with other types of cytochromes c, the conserved histidine residue in this sequence probably provides the fifth ligand to the heme iron.…”

“…Cytochrome c'from Rhodospirillum rubrum consists of a dimer (Afr 27 500) with identical subunits (Meyer et al, 1975).…”