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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Bibliographic Details
Published in:The Journal of biological chemistry 1981-07, Vol.256 (13), p.6617-6622
Main Authors: Bossard, M J, Schuster, S M
Format: Article
Language:English
Subjects:
Adenosine Diphosphate
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate
adenosinetriphosphatase
ADP
Animals
Cattle
chromium (III)
Chromium - pharmacology
heart
Kinetics
mitochondria
Mitochondria, Heart - enzymology
Structure-Activity Relationship
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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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)69034-4