Abstract
Ferredoxin-NADP+ reductase (FNR) catalyzes the electron transfer from ferredoxin to NADP+ via its flavin FAD cofactor. To get further insights in the architecture of the transient complexes produced during the hydride transfer event between the enzyme and the NADP+ coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNRox and the oxidized state of its NADP+ coenzyme. We have found that STD NMR, together with the use of selected mutations on FNR and of the non-FNR reacting coenzyme analogue NAD+, are appropriate tools to provide further information about the the interaction epitope.
NMR Studies of the Stability, Protonation States, and Tautomerism of 13C- and 15N-Labeled Aldimines of the Coenzyme Pyridoxal 5?-Phosphate in Water
NMR Studies of the Stability, Protonation States, and Tautomerism of 13C- and 15N-Labeled Aldimines of the Coenzyme Pyridoxal 5?-Phosphate in Water
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101061m/aop/images/medium/bi-2010-01061m_0010.gif
Biochemistry
DOI: 10.1021/bi101061m
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Linear Mode
