A simplified method is described for the preparation and purification of cytochrome cZ from Rhodspirillum rubrum growth photosynthetically under anaerobic conditions. The cytochrome c1 appeared as a single electrophoretic and chromatographic form at all stages of the preparation.
The reaction of rhodospirillum rubrum cytochrome c2 with iron hexacyanides
β Scribed by Fern E. Wood; Michael A. Cusanovich
- Publisher
- Elsevier Science
- Year
- 1975
- Weight
- 1004 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0006-3061
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β¦ Synopsis
The reaction of Rhodospirillum rubrum cytochrome c2 with the nonphysiological reactants, ferrocyanide and ferricyanide has been investigated as a function of ionic strength, temperature and pH, using both stopped-flow and temperature-jump kinetic methods. The results are consistent with a complex reaction mechanism involving the formation of two intermediate complexes. The site of electron transfer appears to be at the front of the cytochrome c2 molecule near the hem e crevice with interacton of both ferri and ferrocyanide with a positively charged region of the molecule. Comparison of the proposed electron transfer mechanism of cytochrome c2 with ferro-ferricyanide is made with the mechanism proposed based upon structural considerations.
π SIMILAR VOLUMES
The effect of a number of salts on the activity of the particulate NADH-cytochrome c-reductase of Rhodospirillum rubrum was investigated. The enzyme was shown to be inhibited by the presence of these salts. With monovalent anions a relationship between the size of the anion and its capacity of inhib
The nucleotide sequence of the pufoperon of the purple bacterium, Rhodospirillum molischianum, was determined. The operon includes genes coding for the/3 and c~ subunits of the light-harvesting 1 (LH1) complex and the L, M, and cytochrome subunits of the reaction center complex. As in other purple