Biochemical properties and crystal structure of the flavin reductase FerA from Paracoccus denitrificans

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F16%3A00088000" target="_blank" >RIV/00216224:14310/16:00088000 - isvavai.cz</a>

Result on the web

<a href="http://www.sciencedirect.com/science/article/pii/S0944501316301549" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0944501316301549</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.micres.2016.04.006" target="_blank" >10.1016/j.micres.2016.04.006</a>

Result language

angličtina

Original language name

Biochemical properties and crystal structure of the flavin reductase FerA from Paracoccus denitrificans

Original language description

The Pden_2689 gene encoding FerA, an NADH:flavin oxidoreductase required for growth of Paracoccus denitrificans under iron limitation, was cloned and overexpressed as a C-terminally His6-tagged derivative. The binding of substrates and products was detected and quantified by isothermal titration calorimetry and fluorometric titration. FerA binds FMN and FAD with comparable affinity in an enthalpically driven, entropically opposed process. The reduced flavin is bound more loosely than the oxidized one, which was confirmed by a negative shift in the redox potential of FMN after addition of FerA. Initial velocity and substrate analogs inhibition studies showed that FerA follows a random-ordered sequence of substrate (NADH and FMN) binding. The primary kinetic isotope effects from stereospecifically deuterated nicotinamide nucleotides demonstrated that hydride transfer occurs from the pro-S position and contributes to rate limitation for the overall reaction.

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

<a href="/en/project/GAP503%2F12%2F0369" target="_blank" >GAP503/12/0369: Novel flavin-dependent enzymes of Paracoccus denitrificans: reaction mechanisms, metabolic functions and their role in cellular oxidative stress</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Microbiological Research

ISSN

0944-5013

e-ISSN

—

Volume of the periodical

188

Issue of the periodical within the volume

1

Country of publishing house

DE - GERMANY

Number of pages

14

Pages from-to

9-22

UT code for WoS article

000378963100002

EID of the result in the Scopus database

—