Metal-catalyzed Oxidation of Fe2+ Dehydrogenases: consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas Mobilis

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1994
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Cabiscol Català, Elisa
Aguilar, Juan
Ros Salvador, Joaquim
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Cabiscol Català, Elisa; Aguilar, Juan; Ros Salvador, Joaquim; . (1994) . Metal-catalyzed Oxidation of Fe2+ Dehydrogenases: consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas Mobilis. Journal of Biological Chemistry, 1994, Vol. 269, núm. 9, p. 6592-6597. http://hdl.handle.net/10459.1/56772.
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Abstract
We have studied two enzymes of a newly described family of dehydrogenases with high sequence homology, 1,2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. These enzymes perform their metabolic role under anaerobic conditions; in the presence of oxygen, they show a very similar inactivation pattern by a metalcatalyzed oxidation system. Titration of histidine residues with diethyl pyrocarbonate showed one histidine residue less in the oxidized enzymes. Comparison of subtilisin peptide maps of active and inactivated enzymes showed a difference in one histidine-containing peptide, the sequence of which is YNTPH277GVAN for propanediol oxidoreductase and YNLPH277GV for alcohol dehydrogenase 11. This histidine residue lies 10 residues away from a proposed metal-binding site, H263XyXHa67, necessary to explain a site-specific free radical mechanism. The three histidine residues here described are strictly conserved in all enzymes of this family. In this report we propose that histidine 277 is a target for oxidation by a metal-catalyzed oxidation system and that this modification leads to the irreversible inactivation of both enzymes.
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http://hdl.handle.net/10459.1/56772
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Journal of Biological Chemistry, 1994, Vol. 269, núm. 9, p. 6592-6597
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