Kinetics of the membrane-bound inorganic pyrophosphatase from Rhodospirillum rubrum chromatophores
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چکیده
منابع مشابه
Regulatory properties of an inorganic pyrophosphatase from the photosynthic bacterium Rhodospirillum rubrum.
In Rhodospirillum rubrum, inorganic pyrophosphatase activity is observed in both the cytoplasmic and membrane fractions. The soluble enzyme accounts for about 80% of the total activity in crude extracts, and is the subject of this report. Zn(2+) is required for both activity and stability of the enzyme, which has a molecular weight of approximately 90,000 (gel-filtration determinations). The su...
متن کاملThe Photo-oxidation of Succinate by Chromatophores of Rhodospirillum Rubrum.
1. The stoicheiometry of the photo-oxidation of succinate by chromatophores has been investigated with [2,3-(14)C(2)]succinate. It was found that there is a stoicheiometric relationship between the amount of succinate oxidized and the NAD reduced, and that fumarate is the only product of succinate oxidation. 2. The possibility of a direct hydrogen transfer from succinate to NAD in this reaction...
متن کاملPhotooxidase Activity of Heated Chromatophores of Rhodospirillum rubrum.
Van Niel's classical distinction between bacterial and green plant photosyntheses is based on the differences in the metabolism of the photooxidant (16). But direct measurement of the oxidizing power in bacterial photosynthesis is, at best, difficult with the usual spectrophotometric equipment. Light-induced oxidations of endogenous cytochromes have been demonstrated in whole cells and extracts...
متن کاملA disulfide photoreduction system in chromatophores of Rhodospirillum rubrum.
Chromatophores isolated from photosynthetic bacteria contain a disulfide-bonded repeating antigenic substructure that is serologically specific and present on the cell particles only during photosynthetic growth (l-3). This finding suggests that the structural antigen may also be a functional part of the photosynthetic electron transport system. This suggestion has been explored and supported b...
متن کاملPartition kinetics of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum.
When the enzymatically generated intermediate 2-carboxy-3-keto-D-arabinitol-1,5-bisphosphate (II) was used as a substrate with fresh enzyme, 70% reacted to produce 3-phosphoglycerate (3PGA). When a reaction mixture of enzyme plus [1-32P]ribulose 1,5-bisphosphate (RuBP) was quenched in the steady state with the tightly bound inhibitor 2-carboxyarabinitol-1,5-bisphosphate, 30% of the enzyme-bound...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1986
ISSN: 0014-5793
DOI: 10.1016/0014-5793(86)80274-5