Abstract
HUENNEKENS et al.1 purified an erythrocyte fraction containing hæm which was able to catalyse the reduction of methæmoglobin by reduced triphosphopyridine nucleotide in the presence of methylene blue. A single enzyme was believed to be responsible for the electron transport from reduced triphosphopyridine nucleotide to the dye, and from the dye through hæm to methæmoglobin. Although reduced diphosphopyridine nucleotide-cytochrome c reductase from pig heart and reduced triphosphopyridine nucleotide-cytochrome c reductase from yeast do not reduce methæmoglobin, it was shown by Cromier and Rostorfer2 that bacterial extracts with diaphorase activity, as well as milk xanthine oxidase, do reduce methæmoglobin in the presence of methylene blue, suggesting that dia-phorases could also act similarly to methæmoglobin.
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References
Huennekens, F. M., Gaffrey, R. W., Basford, R. E., and Gabrio, J. Biol. Chem., 227, 261 (1957).
Cromier, M. J., and Rosterfer, H. H., Biochim. Biophys. Acta, 22, 292 (1956).
Raw, I., Molinari, R., Amaral, D. F. do, and Mahler, H. R., J. Biol. Chem., 233, 225 (1958). J. Biol. Chem., 233, 225 (1958), ( Mahler, H. R., and Raw, I., unpublished work).
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Lemberg, R., and Legge, J. W., “Hematin Compounds and Bile Pigments”, 745 (Intersci. Pub., New York, 1949).
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PETRAGNANI, N., NOGUEIRA, O. & RAW, I. Methæmoglobin Reduction through Cytochrome B5. Nature 184, 1651 (1959). https://doi.org/10.1038/1841651a0
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DOI: https://doi.org/10.1038/1841651a0
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