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Báo cáo khoa học: A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase
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YhdA, a thermostable NADPH:FMN oxidoreductase fromBacillus subtil-is, reduces quinones via a ping-pong bi-bi mechanism with a pronounced preference for NADPH. The enzyme occurs as a stable tetramer in solu-tion. The two extended dimer surfaces are packed against each other by a 90rotation of one dimer with respect to the other.
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