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

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA204%2F06%2F0944" target="_blank" >GA204/06/0944: Hydrogenosomy trichomonád, elektrontransportní dráhy a rezistence k léčivům</a><br>

Návaznosti

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

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název periodika

Applied biochemistry and biotechnology

ISSN

0273-2289

e-ISSN

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Svazek periodika

153

Číslo periodika v rámci svazku

1-2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

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Kód UT WoS článku

000268308000005

EID výsledku v databázi Scopus

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