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The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium.
The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like
Cytochromes C2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria
The amino acid sequences of the principal soluble cytochromes c of representatives of each recognised species of the Rhodospirillaceae are determined, finding no correlation between a species' cytochrome c amino acid sequence and its phylogenetic position.
Kinetics of photooxidation of soluble cytochromes, HiPIP, and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis.
The photosynthetic reaction center of Rhodopseudomonas viridis contains a bound tetraheme cytochrome c subunit which is the primary electron donor to the photooxidized special pair bacteriochlorophyll and which apparently binds to the reaction center at low ionic strength, as evidenced by a nonlinear dependence of kobs on protein concentration.
The cytochromes of Chlorobium thiosulfatophilum.
Basis for monomer stabilization in Rhodopseudomonas palustris cytochrome c' derived from the crystal structure.
It is suggested that RPCP is monomeric in solution because of the hydrophilic nature of the A-B surface, similar to Rhodobacter capsulatus cytochrome c' (RCCP), which is an equilibrium admixture of monomer and dimer.