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- W2015215659 abstract "A [4Fe–4S]1+ cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. The activator has been proposed to change its conformation by MgATP similarly to nitrogenase Fe-protein. Iron chelation by bathophenanthroline removed the reduced [4Fe–4S]1+ cluster from the activator in an ATP-dependent manner (rate, v = 0.128 ± 0.004 min−1; Km = 21 ± 1 μM); with ADP no chelation was observed (v < 0.001 min−1). Chelation of the oxidised [4Fe–4S]2+ cluster occurred faster with ADP (v = 0.34 ± 0.05 min−1) than with ATP (v = 0.132 ± 0.005 min−1). The data indicate that reduction of the activator and binding of ATP induce conformational changes necessary to transfer the electron to the dehydratase. Interaction of both proteins promotes ATP hydrolysis (Km = 0.5 ± 0.1 μM). Une protéine à centre [4Fe–4S]1+ est capable d'activer la 2-hydroxyisocaproyl-CoA déhydratase par transfert électronique impliquant l'ATP. L'activateur est supposé changer de conformation sous l'influence de MgATP de manière semblable aux nitrogénases (Fe-protéines). La chélation du fer par bathophanthroline entraînait l'enlèvement du centre [4Fe–4S]1+ de l'activateur en dépendance d'ATP (vitesse, v = 0.128 ± 0.004 min−1; Km = 21 ± 1 μM); aucune chélation ne pouvait être observée après traitement avec l'ADP (v < 0.001 min−1). La chélation du centre oxydé [4Fe–4S]2+ se manifestait plus rapidement avec l'ADP (v = 0.34 ± 0.05 min−1) qu'avec l'ATP (v = 0.132 ± 0.005 min−1). Nos résultas indiquent que la réduction de l'activateur et la liaison de l'ATP induisent les changements de conformation nécessaires pour transférer l'électron à la déhydratase. L'interaction des deux protéines favorise l'hydrolyse de ATP (Km = 0.5 ± 0.5 µM)." @default.
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- W2015215659 date "2007-08-01" @default.
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- W2015215659 title "ATP- and redox-induced conformational changes in the activator of the radical enzyme 2-hydroxyisocaproyl-CoA dehydratase" @default.
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- W2015215659 doi "https://doi.org/10.1016/j.crci.2006.12.013" @default.
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