| Literature DB >> 7240187 |
Abstract
Submitochondrial particles from beef heart mitochondria synthesize ADP-arsenate from ADP and arsenate when energized by succinate. The ADP-arsenate formed hydrolyzes rapidly and this is almost certainly the mechanism by which arsenate "uncouples" oxidative phosphorylation. When sufficient hexokinase is present, a substantial portion of the ADP-arsenate formed reacts with glucose to form glucose 6-arsenate and ADP. The glucose 6-arsenate thus formed hydrolyzes, at pH 7.5 and 30 degrees C, under the conditions used, with a rate constant of 5.5 X 10(-4) s-1 and is a substrate for glucose-6-phosphate dehydrogenase.Entities:
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Year: 1981 PMID: 7240187
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157