SOME PROPERTIES OF CYTOCHROME-C AND OTHER HEMOPROTEINS OF THIOCAPSA-ROSEOPERSICINA

Cytochrome c' of Thiocapsa roseopersicina was partially purified by DEAE and Sephadex chromatography (highest purity index A 275 nm ox./A 396 nm ox.=0.54). It is autoxidizable, thermostable, and is located in the soluble fraction. The reduced cytochrome c' reacts with carbon monoxide and has a γ-band at 417 nm and a shoulder at 435 nm. Cyanide (10−2−10−3 M) does not inhibit the reduction of the cytochrome c' by sulfide; only at higher concentrations of cyanide did the shoulder at 435 nm disappear. When the cytochrome c' is reduced by dithionite, only one broad α-band at about 550 nm appears next to the γ-band. When is is reduced by sulfide, the absorption spectrum shows an additional β-band at 521 nm. Cytochrome c' is not reduced by thiosulfate. © 1979, Springer-Verlag New York Inc.. All rights reserved.