Identification of 7-hydroxyindole as an alternative substrate of MauG by in silico and in vitro analysis

Abstract MauG catalyzes the six-electron oxidation of pre-tryptophan tryptophylquinone (preTTQ) cofactor in methylamine dehydrogenase (MADH) to form mature tryptophan (TTQ) via long-range electron transfer. To identify alternative substrates for MauG, docking models 10 tryptophan-like compounds were constructed using Autodock Vina. These demonstrated spontaneous binding preTTQ site with hydroxyindoles most frequently sharing natural substrate MauG. confirm result silico analysis, 7-hydroxyindole was reacted bis -Fe IV The spectroscopic change, representing reactivity revealed highly increased reaction rate ( k 3 ) toward 7-hydroxyindole, suggesting that extracted an from and then oxidized di-ferric