Abstract
WE have been, investigating D-amino-acid oxidase apo-protein, flavin adenine dinucleotide and the substrate with reference to complex formation1,2. In the previous communication1, it was reported that the addition of the apo-protein to flavin adenine dinucleotide causes a shift and decrease of the absorption peak at 450 mµ of the latter. It was also found that the co-existence of benzoate, a substrate-substitute, and the apo-protein causes further marked changes in the absorption spectrum of the flavin, adenine dinucleotide. Two important changes were especially noted : (1) the intensity of the absorption at 450 mµ is further decreased and that at 485 mµ is increased to form a shoulder, and (2) a new absorption peak appears at 465 mµ. These results indicate that both the apo-protein and the benzoate combine with two different binding sites of the isoalloxazine nucleus of flavin adenine dinucleotide. On the other hand, the fact that benzoate competes with the substrate, D-amino-acid3,4, indicates combination between benzoate and the apo-protein. Hence it may be considered that the apo-protein, flavin adenine dinucleotide and benzoate combine to form a tight complex5.
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YAGI, K., OZAWA, T. & HARADA, M. Crystallization of the Complex of D-Amino-Acid Oxidase and Benzoate. Nature 188, 745–746 (1960). https://doi.org/10.1038/188745a0
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DOI: https://doi.org/10.1038/188745a0
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