A STD-NMR study of the interaction of the Anabaena ferredoxin-NAD reductase with the coenzyme

Lara V. Antonini; José R. Peregrina; Jesús Angulo; Milagros Medina; Pedro M. Nieto

doi:10.3390/molecules19010672

A STD-NMR study of the interaction of the Anabaena ferredoxin-NAD reductase with the coenzyme

Lara V. Antonini, José R. Peregrina, Jesús Angulo (Lead Author), Milagros Medina, Pedro M. Nieto

Research output: Contribution to journal › Article › peer-review

16 Downloads (Pure)

Abstract

Ferredoxin-NAD reductase (FNR) catalyzes the electron transfer from ferredoxin to NAD 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 NAD coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNRox and the oxidized state of its NAD coenzyme. We have found that STD NMR, together with the use of selected mutations on FNR and of the non-FNR reacting coenzyme analogue NA, are appropriate tools to provide further information about the the interaction epitope.

Original language	English
Pages (from-to)	672-685
Number of pages	14
Journal	Molecules
Volume	19
Issue number	1
DOIs	https://doi.org/10.3390/molecules19010672
Publication status	Published - 7 Jan 2014

Keywords

saturation transfer difference NMR spectroscopy
flavoenzymes
hydride transfer
isoalloxazine-nicotinamide interactions
CORCEMA-ST

Access to Document

10.3390/molecules19010672Licence: CC BY

Published_VersionFinal published version, 686 KBLicence: CC BY

Cite this

@article{bf862a867ed34922b29d9dc43e87e54f,

title = "A STD-NMR study of the interaction of the Anabaena ferredoxin-NAD reductase with the coenzyme",

abstract = "Ferredoxin-NAD reductase (FNR) catalyzes the electron transfer from ferredoxin to NAD 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 NAD coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNRox and the oxidized state of its NAD coenzyme. We have found that STD NMR, together with the use of selected mutations on FNR and of the non-FNR reacting coenzyme analogue NA, are appropriate tools to provide further information about the the interaction epitope.",

keywords = "saturation transfer difference NMR spectroscopy, flavoenzymes, hydride transfer, isoalloxazine-nicotinamide interactions, CORCEMA-ST",

author = "Antonini, {Lara V.} and Peregrina, {Jos{\'e} R.} and Jes{\'u}s Angulo and Milagros Medina and Nieto, {Pedro M.}",

year = "2014",

month = jan,

day = "7",

doi = "10.3390/molecules19010672",

language = "English",

volume = "19",

pages = "672--685",

journal = "Molecules",

issn = "1420-3049",

publisher = "MDPI AG",

number = "1",

}

TY - JOUR

T1 - A STD-NMR study of the interaction of the Anabaena ferredoxin-NAD reductase with the coenzyme

AU - Antonini, Lara V.

AU - Peregrina, José R.

AU - Angulo, Jesús

AU - Medina, Milagros

AU - Nieto, Pedro M.

PY - 2014/1/7

Y1 - 2014/1/7

N2 - Ferredoxin-NAD reductase (FNR) catalyzes the electron transfer from ferredoxin to NAD 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 NAD coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNRox and the oxidized state of its NAD coenzyme. We have found that STD NMR, together with the use of selected mutations on FNR and of the non-FNR reacting coenzyme analogue NA, are appropriate tools to provide further information about the the interaction epitope.

AB - Ferredoxin-NAD reductase (FNR) catalyzes the electron transfer from ferredoxin to NAD 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 NAD coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNRox and the oxidized state of its NAD coenzyme. We have found that STD NMR, together with the use of selected mutations on FNR and of the non-FNR reacting coenzyme analogue NA, are appropriate tools to provide further information about the the interaction epitope.

KW - saturation transfer difference NMR spectroscopy

KW - flavoenzymes

KW - hydride transfer

KW - isoalloxazine-nicotinamide interactions

KW - CORCEMA-ST

UR - http://www.scopus.com/inward/record.url?scp=84893070012&partnerID=8YFLogxK

U2 - 10.3390/molecules19010672

DO - 10.3390/molecules19010672

M3 - Article

AN - SCOPUS:84893070012

SN - 1420-3049

VL - 19

SP - 672

EP - 685

JO - Molecules

JF - Molecules

IS - 1

ER -

A STD-NMR study of the interaction of the Anabaena ferredoxin-NAD reductase with the coenzyme

Abstract

Keywords

Access to Document

Other files and links

Jesus Angulo

Cite this

A STD-NMR study of the interaction of the Anabaena ferredoxin-NAD reductase with the coenzyme

Abstract

Keywords

Access to Document

Other files and links

Profiles

Jesus Angulo

Cite this