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A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.

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.

SUBMITTER: Antonini LV

PROVIDER: S-EPMC6272016 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.

Antonini Lara V LV Peregrina José R JR Angulo Jesús J Medina Milagros M Nieto Pedro M PM

Molecules (Basel, Switzerland) 20140107 1

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 o ...[more]

PMID: 24402199

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