Summary
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1.
The photochemical reversibility of carbon monoxide inhibition of the tryptophan 2,3-dioxygenase of the blowflyProtophormia terrae-novae (Fig. 1) strongly indicates the heme-protein nature of the enzyme.
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2.
The effects of both the substrates, tryptophan and oxygen, respectively, on each other's affinity to the enzyme were studied. There is no change in S(0.5) for tryptophan with varying oxygen pressure (Fig. 2). On the other hand, S(0.5) for oxygen decreases markedly with increasing tryptophan concentrations (Fig. 3).
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Schartau, W. The tryptophan 2,3-dioxygenase of the blowflyProtophormia terrae-novae: Inhibition by carbon monoxide, and interaction between oxygen and tryptophan binding sites. J Comp Physiol B 124, 117–119 (1978). https://doi.org/10.1007/BF00689171
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DOI: https://doi.org/10.1007/BF00689171