Biochemistry and Cell Biology (Impact Factor: 2.15). 02/2011; 37(8):1049-1067. DOI: 10.1139/y59-113


The oxidation of solutions of ascorbic acid catalyzed by copper and the copper complexes of amino acids, peptides, and proteins has been investigated by manometric and chemical means. The copper-containing solutions were prepared by equilibration with the sparingly soluble salt malachite. The catalytic activity of the complexed copper was found to be dependent upon the type of complexing molecule. For amino acids the more firmly bound copper atoms tended to be the best catalysts. The catalytic activity of the copper complexed to several glycine peptides was approximately one half of the mean value of that of the copper complexed to amino acids. The catalytic activity of copper complexed to bovine plasma albumen and pepsin was lower than that of copper complexed with amino acids or peptides. The more firmly bound copper atoms on pepsin showed a higher catalytic activity than the mean value for all the complexed copper atoms. Sodium chloride markedly reduced the catalytic activity of both free copper and complexed copper. In the absence of sodium chloride free copper was 10 times as effective a catalyst as copper complexed to glycine. In the presence of 0.178 M sodium chloride the complexed copper was twice as effective as free copper.

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    ABSTRACT: A comprehensive survey of the interaction of the copper proteins and oxygen is presented including a correlation of structure, function, and other properties of the known copper oxidases and of hemocyanin. The origin of their blue color and the structure of copper complexes and copper proteins are related to the oxidation state of copper ion and relevant electronic transitions probably arising from the formation of charge transfer complexes. The oxygen reactions of hemocyanin, ceruloplasmin, and cytochrome oxidase show half-saturation values far below the other Cu enzymes. The formation of hydrogen peroxide as a reaction product is associated with the presence of one Cu atom per oxidase molecule or catalytic system. Water is the corresponding product of the other Cu oxidases with four or more Cu atoms per molecule, except for monoamine oxidase. Mechanisms for the oxidase action of the two and four electron transfer Cu oxidases and tyrosinase are proposed. These reactions account for the number, the oxidation-reduction potential, and the oxidation state of Cu in the resting enzyme, the cyclical change from Cu(II) to Cu(I), the diatomic nature of O(2), the sequence of the oxidation and reduction reactions, and other salient features. The catalytic reactions involved in the oxidation of ascorbic acid by plant ascorbate oxidase, ceruloplasmin, and Cu(II) are compared. Finally the substrate specificity, inhibitory control, and the detailed mechanism of the oxidase activity of ceruloplasmin are summarized.
    Preview · Article · Oct 1965 · The Journal of General Physiology
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    ABSTRACT: Zimmerman, Leonard (Fort Detrick, Frederick, Md.). Toxicity of copper and ascorbic acid to Serratia marcescens. J. Bacteriol. 91:1537-1542. 1966.-Neutral solutions of ascorbic acid were antibacterial to Serratia marcescens at low but not at high population densities. The toxicity of ascorbate was eliminated by metal-sequestering treatments, and was restored only by the addition of trace amounts of copper salts. Copper-ascorbate was equally toxic under aerobic or anaerobic conditions; its toxicity was abolished by (i) chelating agents that sequestered the copper, (ii) metal-complexing agents that bound to the cells but did not sequester copper, and (iii) iron salts in the presence of air. On the basis of these observations, the toxic effects of copper-ascorbate were attributed to its reaction with vital Fe-containing cellular components.
    Preview · Article · May 1966 · Journal of Bacteriology
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    ABSTRACT: Neutralized ascorbic acid (AA), buffered or unbuffered and autoclaved or filter-sterilized, was sporicidal for Clostridium. A 0.2% concentration of AA was generally employed, and spore counts were made in a soft-agar modification of Wynne's medium in Prickett tubes. Spores of Clostridium botulinum 115B were less susceptible than those of C. sporogenes PA 3679, whereas C. bifermentans spores were by far the most sensitive. At 75 C, spores of PA 3679 were killed at a rate of about 9% at 0 min (warm-up) to 99+% at 100 min. The lower the temperature, the longer the time needed for a given lethality. The percentage of killing increased with increasing concentrations of AA, and the rate of killing was lower at a higher concentration of spores. At least two mechanisms were operative: a major mechanism involving a product(s) of AA auto-oxidation, and a minor mechanism involving copper-ascorbate toxicity. AA reduced in natural gas was not sporicidal after 18.5 hr at 25 C, whereas 92% of the spores were killed by oxidized AA. Although H(2)O(2) per se was sporicidal, catalase did not reverse lethality of fresh or oxidized AA. Dehydroascorbate was as sporicidal as any AA preparation. Added copper (0.00001%) increased the rate of lethality of freshly prepared AA from 66 to 83% but was not effective with thoroughly oxidized AA. Ethylenediaminetetraacetic acid, NH(4) (+), and phosphate partially reversed AA toxicity, deionized water had no effect, and complex media, as well as thioglycolate, eliminated AA lethality. Since the percentage of killing was affected by spore concentration, AA did not seem to stimulate "lethal germination."
    Preview · Article · Mar 1968 · Applied microbiology
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