. Bioenergetics. Bioenergetics. 71 electrons which could transport energy, the purine having its system of conjugated double bonds and the phosphate the O's with their nonbonded lone pairs of electrons. The P—O—P, which represents the (£), could merge thus with the adenine in one extensive system of mobile electrons. This opens the possibility that when such a double chelate is formed and the metal attracts electrons from the phosphates, it. V^v^ Fig. 19. Mg chelate of c-phenylenediamine and naphthoquinone. decreases the energy^ and strength of the P—O—P bond, which then falls prey to hydrolyt
. Bioenergetics. Bioenergetics. 71 electrons which could transport energy, the purine having its system of conjugated double bonds and the phosphate the O's with their nonbonded lone pairs of electrons. The P—O—P, which represents the (£), could merge thus with the adenine in one extensive system of mobile electrons. This opens the possibility that when such a double chelate is formed and the metal attracts electrons from the phosphates, it. V^v^ Fig. 19. Mg chelate of c-phenylenediamine and naphthoquinone. decreases the energy^ and strength of the P—O—P bond, which then falls prey to hydrolytic splitting while its energy appears in the purine ring as E*, completing the (E) -> £* transformation. That Mg can actually facilitate the passage of electrons from one substance to another with which this metal forms complexes can be demonstrated by mixing an alcoholic solution of 1,2-naph- thoquinone and (9-phenylenediamine (Fig. 19). In this system the quinone oxidizes the diamine very slowdy, electrons passing from the latter to the former. This reaction is greatly speeded up by Mg, in analogy to the ATP-ase activity of myosin, which also can occur without Mg, but is greatly accelerated by the metal. The reaction between quinone and diamine is indicated by the darkening of the solution (w^hich can readily be reverted by reducing agents such as ascorbic acid). One attractive feature of this theory of ATP-ase activity is that it is analogous to E. L. Smith's theory of peptidase Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Szent-Györgyi, Albert, 1893-1986. New York, Academic Press
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