2006
DOI: 10.1016/j.jinorgbio.2006.08.007
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A role for copper in biological time-keeping

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Cited by 10 publications
(19 citation statements)
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References 39 publications
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“…Maxima r and s were more widely separated than the others. copper but appear to be inherent in the molecular structure of the Cu II aqua ion [3] itself. Solvated Cu II as the chloride or other salts alone exhibit the property of catalysis of NADH oxidation.…”
Section: Introductionmentioning
confidence: 99%
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“…Maxima r and s were more widely separated than the others. copper but appear to be inherent in the molecular structure of the Cu II aqua ion [3] itself. Solvated Cu II as the chloride or other salts alone exhibit the property of catalysis of NADH oxidation.…”
Section: Introductionmentioning
confidence: 99%
“…With Cu II Cl 2 , the pattern also consists of 5 maxima, two of which are separated by an interval of 6 min and three which are separated by intervals of 4.5 min. The total period length is 24 min and the period length is independent of temperature and pH [3].…”
Section: Introductionmentioning
confidence: 99%
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“…Organisms grown in D2O consistently exhibit circadian periods of about 30 h compared to the normal period length of 24 h [8]. Further studies revealed a requirement for bound copper II to sustain the periodicity of the ENOX proteins [9,10]. When examined in the absence of protein, copper II hexahydrate in aqueous solution also revealed oscillatory changes in redox potential sufficient to catalyze the oxidation of NADH with a period length of 24 min.…”
Section: Time-keeping Enox Proteinsmentioning
confidence: 94%
“…All ENOX proteins require bound Cu II for activity [9,10]. Activity is lost when the ENOX proteins are unfolded in the presence of the copper chelator bathocuproine and then refolded.…”
Section: Time-keeping Enox Proteinsmentioning
confidence: 99%