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Structural preferences for the binding of chromium nucleotides by beef heart mitochondrial ATPase
The mono- and bidentate forms of adenosine 5'-diphosphate, chromium (III) salt (CrADP) were separated using Sephadex G-10 column chromatography. The isomeric purity of the two forms was monitored using high voltage electrophoresis and column chromatography. The same techniques were employed to...
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Published in: | The Journal of biological chemistry 1981-07, Vol.256 (13), p.6617-6622 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The mono- and bidentate forms of adenosine 5'-diphosphate, chromium (III) salt (CrADP) were separated using Sephadex G-10
column chromatography. The isomeric purity of the two forms was monitored using high voltage electrophoresis and column chromatography.
The same techniques were employed to assess the purity of the mono-, bi-, and tridentate forms of adenosine 5'-triphosphate,
chromium (III) salt (CrATP). Distinct differences in the interaction of beef heart mitochondrial ATPase with the various isomers
of chromium nucleotides were seen in kinetic studies. Monodentate CrADP was a competitive inhibitor of the ATP hydrolysis
activity of both purified ATPase and submitochondrial particles. However, when ITPase activity was examined, noncompetitive
inhibition was observed. The bidentate isomer of CrADP did not affect ATPase activity. Enzymatic synthesis of the transition
state analog of ATP synthesis and hydrolysis, Pi-CrADP occurred exclusively with the monodentate isomer of CrADP. It was also
found that only the mono- and tridentate forms of CrATP were potent inhibitors of ATP hydrolysis by beef heart mitochondrial
ATPase. These results are discussed in terms of possible ATP synthesis and hydrolysis mechanisms. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)69034-4 |