Engineering Escherichia coli for Fermentative Dihydrogen Production: Potential Role of NADH-F Oxidoreductase from the Hydrogenosome of Anaerobic Protozoa

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F09%3A10000735" target="_blank" >RIV/00216208:11310/09:10000735 - isvavai.cz</a>

Result on the web

—

DOI - Digital Object Identifier

—

Result language

angličtina

Original language name

Engineering Escherichia coli for Fermentative Dihydrogen Production: Potential Role of NADH-F Oxidoreductase from the Hydrogenosome of Anaerobic Protozoa

Original language description

Trichomonas vaginalis generates reduced ferredoxin within a unique subcellular organelle, hydrogenosome that is used as a reductant for H-2 production. Pyruvate ferredoxin oxidoreductase and NADH dehydrogenase (NADH-DH) are the two enzymes catalyzing theproduction of reduced ferredoxin. The genes encoding the two subunits of NADH-DH were cloned and expressed in Escherichia coli. Kinetic properties of the recombinant heterodimer were similar to that of the native enzyme from the hydrogenosome. The recombinant holoenzyme contained 2.15 non-heme iron and 1.95 acid-labile sulfur atoms per heterodimer. The EPR spectrum of the dithionite-reduced protein revealed a [2Fe-2S] cluster with a rhombic symmetry of g(xyz)=1.917, 1.951, and 2.009 corresponding to cluster N1a of the respiratory complex I. Based on the Fe content, absorption spectrum, and the EPR spectrum of the purified small subunit, the [2Fe-2S] cluster was located in the small subunit of the holoenzyme. This recombinant NADH-DH ox

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/GA204%2F06%2F0944" target="_blank" >GA204/06/0944: Trichomonad hydrogenosomes, electrontransporting pathways and drug resistance</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2009

Confidentiality

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

Name of the periodical

Applied biochemistry and biotechnology

ISSN

0273-2289

e-ISSN

—

Volume of the periodical

153

Issue of the periodical within the volume

1-2

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

—

UT code for WoS article

000268308000005

EID of the result in the Scopus database

—