| 1 | Author
| HansWerner Miiller, Margareta Baltscheffsky | Requires cookie* | | Title
| On the Oligomycin-Sensitivity and Subunit Composition of the ATPase Complex from Rhodospirillum rubrum  | | | Abstract
| Two alternative procedures for isolation of the oligomycin-sensitive ATPase complex (E. C. 3.6.1.3) from R. rubrum chromatophores are compared with respect to ease, rapidity, and yield. The inhibitory effect of oligomycin on the membrane-bound Ca2+ -ATPase activity is increased during storage of the chromatophores, whereas the effect of oligomycin on the membrane-bound Mg2+ -ATPase activity does not change within a week. Oligomycin-sensitivity of the solubilized ATPase complex depends on the isolation procedure. The enzyme complex consists of at least nine different polypeptides with the apparent molec ular weights of (. The polypeptides 2 — 4, 7, and 8 represent subunits of coupling factor 1. | | |
Reference
| Z. Naturforsch. 34c, 229 (1979); received January 4 1979 | | |
Published
| 1979 | | |
Keywords
| Rhodospirillum rubrum, ATPase, Subunits, Oligomycin | | |
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| default:Reihe_C/34/ZNC-1979-34c-0229.pdf | | | Identifier
| ZNC-1979-34c-0229 | | | Volume
| 34 | |
2 | Author
| HansW. Erner Müller, Udo Schwuléra, Manfred Salzer, Klaus Dose | Requires cookie* | | Title
| Purification, Subunit Structure, and Kinetics of the Chloroform-Released FjATPase Complex from Rhodospirillum rubrum and Its Comparison with FjATPase Forms Isolated by Other Methods  | | | Abstract
| A stable and homogeneous adenosine-5'-triphosphatase (ATPase, EC 3.6.1.3) has been solubilized from R hodospirillum rubrum (R . rubrum) chromatophores by chloroform extraction. Purification of the Ca2+-dependent ATPase activity was 200-fold. Ca2+ can be replaced by M g2+, Cd2+, and M n2+ .The K m for Ca-ATP (0.17 m M) is increased about 5-fold during solubilization of the enzyme, whereas the K m values for Mg-ATP (0.029 m M) and Cd-ATP (0.014 m M) are not affected. The chloroform-released A TPase has a molecular weight of 400,000 + 30,000 and consists of the following subunits (m olecular weights in parenthesis): a (58,000), ß (53,500), y (39,000), 6(18,500), and £(14,000). The amino acid composition and the fluorescence spectra are presented. Besides the chloroform-released A TPase complex three other Ca2+-dependent A T Pase forms have been isolated from R. rubrum chromatophores by other methods for comparison. Ultrasonica-tion of the m em branes leads to the release of an ATPase complex which is m ainly composed of a, ß , and 7 -subunits. From an acetone powder extract an A TPase complex could be purified by affinity chromatography which is composed of four kinds of subunits (a, ß , y, 6). The same acetone powder yields an A TPase consisting of only three different types of subunits (a, ß, y) if the final purification step is preparative disc electrophoresis on 6% polyacrylam ide gels instead of affinity chromatography. | | |
Reference
| Z. Naturforsch. 34c, 38 (1979); received November 10 1978 | | |
Published
| 1979 | | |
Keywords
| Rhodospirillum rubrum, F xA TPase Complexes, Subunit Structure, Kinetics | | |
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| default:Reihe_C/34/ZNC-1979-34c-0038.pdf | | | Identifier
| ZNC-1979-34c-0038 | | | Volume
| 34 | |
3 | Author
| Z. Naturforsch | Requires cookie* | | Title
| The Rieske Protein from Purple Sulfur Bacteria Is an Extrinsic Protein  | | | Abstract
| The mode of membrane attachment of the Rieske iron-sulfur protein from cytochrome be, complex of Rhodospirillum rubrum has been studied using biochemical approaches. In contrast to cytochrome c, the bacterial Rieske protein was extracted from chromato-phores using chaotropic agents (NaSCN, urea, guanidine), an alkaline pH and relatively low concentration of Triton X-100. The results presented here lead to the conclusion, that the Rieske protein from chromato-phores is extrinsic and that their association with the rest of the complex involves hydropho bic interactions. In tro d u ctio n | | |
Reference
| Z. Naturforsch. 53c, 15—20 (1998); received September 30/0ctober 16 1997 | | |
Published
| 1998 | | |
Keywords
| Chrom atophor, Cytochrome be, Complex, Rieske Protein, Rhodospirillum rubrum | | |
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| default:Reihe_C/53/ZNC-1998-53c-0015.pdf | | | Identifier
| ZNC-1998-53c-0015 | | | Volume
| 53 | |
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