Letter | Published:

Transfer of Phosphate by Coenzyme I

Nature volume 158, page 746 (23 November 1946) | Download Citation

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Abstract

IN 1938, Ostern et al.1 put forward a hypothesis according to which the function of coenzyme I is to transfer phosphate. It was suggested that the coenzyme in muscle, while taking up two hydrogen atoms in the pyridine nucleus through the addition of free phosphate, undergoes a phosphorolysis and is split into pyridin nucleotide and adenosine diphosphoric or triphosphoric acid. After the splitting off of phosphate, the adenine part of the coenzyme molecule recombines with the pyridine nucleotide part. In yeast, however, this mechanism was assumed to function in a somewhat different way, on account of the ability of the yeast enzyme to phosphorylate adenosine. Here also the hydrogenation would be accompanied by a hydrolysis of the coenzyme molecule followed by a transfer of the phosphate of the adenylic acid to other phosphate acceptors. In the regeneration of the coenzyme molecule occurring through the dehydrogenation of the pyridine nucleus, inorganic phosphate is said to be taken up. The validity of this hypothesis was tested in experiments in vitro by Meyerhof et al.2. With the aid of radioactive phosphate they showed that the coenzyme I did not incorporate phosphate either at the hydrogen transfer or at the phosphate transfer.

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References

  1. 1.

    , , and , Z. physiol. Chem., 251, 258 (1938).

  2. 2.

    , , , and , Biochem. Z., 298, 396 (1938).

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Affiliations

  1. Wenner Grens Institute for Experimental Biology, University of Stockholm. Oct. 13.

    • P. E. LINDAHL
    • , B. STRINDBERG
    • , M. MALM
    •  & B. M. LAGERGREN

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DOI

https://doi.org/10.1038/158746a0

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