Thermostability and activation by divalent cations of the membrane-bound inorganic pyrophosphatase of Rhodospirillum rubrum |
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| Institution: | 1. ERC Advanced Investigator Grant Research Group at the Institute for Physiological Chemistry, University Medical Center of the Johannes Gutenberg University Mainz, Germany;1. Glyn O. Phillips Hydrocolloid Research Centre, School of Bioengineering and Food Science, Hubei University of Technology, Wuhan 430068, China;2. Ferguson (Wuhan) Biotechnologies Ltd., Wuhan 430056, China;3. School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China |
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| Abstract: | - 1.1. The activation energy of the membrane bound H+-pyrophosphatase is 44.9 k J·mol?1, for the detergent solubilized enzyme is 55.9 kJ·mol?1.
- 2.2. The Arrhenius plots obtained for pyrophosphatases of Rhodospirillum rubrum show no breaks.
- 3.3. At 70°C, the membrane-bound pyrophosphatase is more stable in the presence of either Mg2+ or Zn2+ than in their absence.
- 4.4. At 65°C, an activator effect of Mg2+ or Zn2+ was observed. Nevertheless, at 70°C no activation was obtained.
- 5.5. The activator effects of Mg2+ or Zn2+ were depended of their concentration.
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