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Manuel Hervás, Qamar Bashir, Nicole G. H. Leferink, Patricia Ferreira, Blas Moreno-Beltrán, Adrie H. Westphal, Irene Dίaz–Moreno, Milagros Medina, Miguel A. de la Rosa, Marcellus Ubbink, José A. Navarro and Willem J. H. van Berkel Communication between L–galactono–1,4–lactone dehydrogenase and cytochrome c The FEBS Journal 280

Version of Record online: 25 MAR 2013 | DOI: 10.1111/febs.12207

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l-galactono-1,4-lactone dehydrogenase (GALDH) catalyzes the terminal step of vitamin C biosynthesis in plant mitochondria. GALDH communicates with its natural electron acceptor cytochrome c (Cc) via a low-affinity interaction, similar for all partner redox states, involving protein-protein dynamic motions. Evidence is also provided that Cc utilizes a conserved surface surrounding the heme edge for interaction with GALDH and other redox partners.

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