Interaction of Chromatium vinosum flavocytochrome c‐552 with cytochromes c studied by affinity chromatography

FEBS Letters

Gray, Gary O.¹  Davidson, Michael W.¹  Knaff, David B.¹ 

[1] Department of Chemistry, Texas Tech University, Lubbock, TX 79409, USA

关键词: Flavocytochrome c-552 Chromatium vinosum Cytochrome c Affinity chromatography;   

DOI  :  10.1016/0014-5793(85)81233-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Flavocytochrome c-552, isolated from the photosynthetic purple sulfur bacterium Chromatium vinosum, after linkage to an Affigel 10-affinity matrix, will bind equine and yeast mitochondrial cytochromes c, C. vinosum cytochrome c-550 and cytochrome c ₂ from the photosynthetic purple non-sulfur bacterium Rhodo-pseudomonas viridis. Similarly, an equine cytochrome c-Sepharose 4B affinity column will bind the C. vinosum flavocytochrome c-552 and its separated heme-containing subunit. These results and the correlation between the effect of ionic strength on binding of the flavocytochrome c-552 to cytochrome c and on the sulfide:cytochrome c oxidoreductase activity catalyzed by C. vinosum flavocytochrome c-552 support the idea of the involvement of an electrostatic complex between the two proteins during sulfide oxidation.

【 授权许可】

Unknown