Comparative solvent perturbation of horse heart cytochrome c and Rhodospirillum rubrum cytochrome c2.

The reaction domain on Rhodospirillum rubrum cytochrome c2 and horse cytochrome c for the Rhodospirillum rubrum cytochrome bc1 complex.

The interaction of the Rhodospirillum rubrum cytochrome bc1 complex with R. rubrum cytochrome c2 and horse cytochrome c was studied using specific lysine modification and ionic strength dependence methods. In order to define the reaction domain on cytochrome c2, several fractions consisting of mixtures of singly labeled carboxydintrophenyl-cytochrome c2 derivatives were employed. Fraction A con...

Oxidation of c-Type Cytochromes by the Membrane-Bound Cytochrome Oxidase (Cytochrome aa(3)) of Blue-Green Algae.

Respiratory particles containing an aa(3)-type cytochrome oxidase were prepared from Anacystis nidulans, Synechocystis 6714, Synechococcus lividus, Anabaena variabilis, Nostoc sp. strain MAC, Nostoc muscorum, and Mastigocladus laminosus. Oxidation of c-type cytochromes by membrane preparations of the different blue-green algae was observed using purified cytochromes from horse heart, Candida kr...

Reactions of Rhodospirillum rubum extract with cytochrome c and cytochrome c2.

Observations from a number of different experimental approaches have implicated cytochrome pigments in oxidation-reduction reactions resulting from the illumination of photosynthetic tissues (l-6). Possible relationships of these cytochromes to those of the respiratory chain pigments which react with oxygen in the dark have been considered. Vernon (7) isolated a soluble cytochrome in good yield...

The structure of oxidized cytochrome c 2 of Rhodospirillum rubrum.

Amino Acid Sequence of Cytochrome c’ from the Purple Photosynthetic Bacterium Rhodospirillum rubrum Sl*

The amino acid sequence of cytochrome c’ from the purple photosynthetic bacterium Rhodospirillum rubrum Sl has been determined and is consistent with homology to cytochrome c’ from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c’ is composed of a single peptide chain of 126 amino acid residue...