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Éva Gráczer, Corinne Lionne, Péter Závodszky, Laurent Chaloin and Mária Vas Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase The FEBS Journal 280

Version of Record online: 11 MAR 2013 | DOI: 10.1111/febs.12191

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The time course of NADH production during the pre-steady state of 3-isopropylmalate dehydrogenase (IPMDH) catalysed reaction, followed by the fast kinetic method quenched flow (QF), is possibly limited by the occurrence of substrate-caused protein conformational change(s), e.g. domain closure, as reflected by formation of a FRET (fluorescence resonance energy transfer) signal between protein tryptophan(s) and the bound NADH.

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