Reconstitution of energy-linked activities of the solubilized F1F0 ATP synthase from Bacillus subtilis
| Autor: | Terry A. Krulwich, D M Cohen, David Hicks |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Carbonyl Cyanide m-Chlorophenyl Hydrazone
Proteolipids Protein subunit Mutant Bacillus subtilis Carbonyl cyanide m-chlorophenyl hydrazone Microbiology Phosphates chemistry.chemical_compound Adenosine Triphosphate ATP hydrolysis Molecular Biology chemistry.chemical_classification biology Hydrolysis Proton Pumps biology.organism_classification Bacillales Proton-Translocating ATPases Enzyme Biochemistry chemistry Energy Metabolism Peptides Adenosine triphosphate Research Article |
| Zdroj: | Journal of Bacteriology. 176:4192-4195 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | The F1F0 ATP synthases from wild-type Bacillus subtilis and an uncoupler-resistant mutant have comparable subunit structures. In accord with an earlier hypothesis, ATP hydrolysis and ATP-Pi exchange by the two synthases were equally stimulated and inhibited by protonophores, respectively, when reconstituted alone in either wild-type or mutant lipids. |
| Databáze: | OpenAIRE |
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