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標題: Essential role of copper in the activity and regular periodicity of a recombinant, tumor-associated, cell surface, growth-related and time-keeping hydroquinone (NADH) oxidase with protein disulfide-thiol interchange activity (ENOX2)
作者: Tang, X.Y.
Chueh, P.J.
Jiang, Z.Y.
Layman, S.
Martin, B.
Kim, C.
Morre, D.M.
Morre, D.J.
關鍵字: Hydroquinone (NADH) oxidase;tNOX or ENOX2;Copper;Biological clock;Growth;plasma-membranes;hela-cells;molecular-cloning;cancer;capsaicin;tnox;complex;culture;site;nox
Project: Journal of Bioenergetics and Biomembranes
期刊/報告no:: Journal of Bioenergetics and Biomembranes, Volume 42, Issue 5, Page(s) 355-360.
ECTO-NOX proteins are growth-related cell surface proteins that catalyze both hydroquinone or NADH oxidation and protein disulfide interchange and exhibit time-keeping and prion-like properties. A bacterially expressed truncated recombinant 46 kDa ENOX2 with full ENOX2 activity bound ca 2 moles copper and 2 moles of zinc per mole of protein. Unfolding of the protein in trifluoroacetic acid in the presence of the copper chelator bathocuproine resulted in reversible loss of both enzymatic activities and of a characteristic pattern in the Amide I to Amide II ratios determined by FTIR with restoration by added copper. The H546-V-H together with His 562 form one copper binding site and H582 represents a second copper site as determined from site-directed mutagenesis. Bound copper emerges as having an essential role in ENOX2 both for enzymatic activity and for the structural changes that underly the periodic alternations in activity that define the time-keeping cycle of the protein.
ISSN: 0145-479X
DOI: 10.1007/s10863-010-9305-8
Appears in Collections:生物醫學研究所

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