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Structure
1.8.5.3
2-n-heptyl-4-hydroxyquinoline N-oxide
residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the binding of the MQH2 inhibitor analogue 2-n-heptyl-4-hydroxyquinoline N-oxide
1.8.5.3
2-n-heptyl-4-hydroxyquinoline-N-oxide
menaquinol analogue. 2-n-Heptyl-4-hydroxyquinoline-N-oxide fluorescence is quenched when 2-n-heptyl-4-hydroxyquinoline-N-oxide binds to the holoenzyme DmsABC. The binding stoichiometry is about 1:1. There is one high-affinity 2-n-heptyl-4-hydroxyquinoline-N-oxide binding site per DmsABC molecule located in the DmsC subunit. The interaction follows a two-step equilibrium model, a fast bimolecular step followed by a slow unimolecular step. The quenching of 2-n-heptyl-4-hydroxyquinoline-N-oxide fluorescence occurs in the bimolecular step
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