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Title: Identification of essential amino-acid residues in Azotobacter vinelandii isocitrate dehydrogenase by radical anions and H atoms

Journal Article · · Radiat. Res.; (United States)
DOI:https://doi.org/10.2307/3574986· OSTI ID:5341643

Pure TPN/sup +/-specific isocitrate dehydrogenase from Azotobacter vinelandii was irradiated with H atoms generated in a ..gamma..-irradiated solution at pH 6.5. A G(-activity) = 0.12 +- 0.01 was found. At the same time no corresponding loss in free sulfhydryls was observed. These results confirmed the essentiality of methionine for the enzymatic activity as known from previous studies. Irradiation with the radical anions, (CNS)/sub 2/- and Br/sub 2//sup -/ generated in ..gamma..-irradiated solutions at pH 6.5, strongly inactivated isocitrate dehydrogenase with yields of G(-activity) of 2.1 and 3.9, respectively. Part of the inactivating effect, however, is due to oxidation of sulfhydryl groups. These results lead to the conclusion that tryptophan is an essential amino-acid residue to isocitrate dehydrogenase from A. vinelandii. The presence of tryptophan in the enzyme was demonstrated by pulse radiolysis.

OSTI ID:
5341643
Journal Information:
Radiat. Res.; (United States), Vol. 80:3
Country of Publication:
United States
Language:
English

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