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Some properties of cytochromec' and other hemoproteins ofThiocapsa roseopersicina

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Abstract

Cytochromec' ofThiocapsa 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 cytochromec' 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 cytochromec' by sulfide; only at higher concentrations of cyanide did the shoulder at 435 nm disappear. When the cytochromec' 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. Cytochromec' is not reduced by thiosulfate.

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  1. Institut für Mikrobiologie, Universität Bonn, Meckenheimer Allee 168, D-5300, Bonn 1, Federal Republic of Germany

    Ulrich Fischer & Hans G. Trüper

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  1. Ulrich Fischer
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  2. Hans G. Trüper
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Fischer, U., Trüper, H.G. Some properties of cytochromec' and other hemoproteins ofThiocapsa roseopersicina . Current Microbiology 3, 41–44 (1979). https://doi.org/10.1007/BF02603132

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