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Kinetics of chromium nucleotide isomer interconversion
Journal of Inorganic Biochemistry
|August 1, 1982
Summary
Chromium nucleotide isomer interconversion rates depend on pH, ionic strength, and temperature. Optimal stability for chromium adenosine 5'-monophosphate (CrADP) complexes occurs at pH 3.5 and 4°C.
Area of Science:
- Biochemistry
- Chemical Kinetics
- Coordination Chemistry
Background:
- Chromium nucleotide complexes play roles in biological systems.
- Understanding isomer interconversion is crucial for elucidating reaction mechanisms.
Purpose of the Study:
- To investigate the kinetics of chromium nucleotide isomer interconversion.
- To determine the influence of pH, ionic strength, and temperature on these rates.
Main Methods:
- High voltage electrophoresis for nucleotide isomer separation.
- Gel filtration chromatography for purification and analysis.
- Kinetic studies under varying environmental conditions.
Main Results:
- Conversion rate of monodentate to bidentate chromium adenosine 5 omino-monophosphate (CrADP) increased with pH, temperature, and ionic strength.
- Optimal CrADP complex stability observed at pH 3.5 and 4°C.
- Rapid decomposition of chromium complexes above pH 7.0, even at 4°C.
Conclusions:
- Isomer interconversion involves proton removal.
- Activation energy for conversion at pH 6.5 is 7.3 kcal/mol.
- Kinetics support proposed conversion mechanisms for chromium nucleotide isomers.