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

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
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 the production 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 oxidized NADH
  • 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 the production 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 oxidized NADH (en)
Title
  • Engineering Escherichia coli for Fermentative Dihydrogen Production: Potential Role of NADH-F Oxidoreductase from the Hydrogenosome of Anaerobic Protozoa
  • Engineering Escherichia coli for Fermentative Dihydrogen Production: Potential Role of NADH-F Oxidoreductase from the Hydrogenosome of Anaerobic Protozoa (en)
skos:prefLabel
  • Engineering Escherichia coli for Fermentative Dihydrogen Production: Potential Role of NADH-F Oxidoreductase from the Hydrogenosome of Anaerobic Protozoa
  • Engineering Escherichia coli for Fermentative Dihydrogen Production: Potential Role of NADH-F Oxidoreductase from the Hydrogenosome of Anaerobic Protozoa (en)
skos:notation
  • RIV/00216208:11310/09:10000735!RIV10-GA0-11310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA204/06/0944), Z(MSM0021620858)
http://linked.open...iv/cisloPeriodika
  • 1-2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 313265
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11310/09:10000735
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Complex-i; quinone oxidoreductase; spectrophotometric determination; paracoccus-denitrificans; trichomonas-vaginalis; h-2 metabolism; cyanobacteria; expression; energy; acid (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [2F32DEE204F3]
http://linked.open...i/riv/nazevZdroje
  • Applied biochemistry and biotechnology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 153
http://linked.open...iv/tvurceVysledku
  • Hrdý, Ivan
  • Šafaříková, Lucie
  • Angerhofer, Alexander
  • Do, Phi Minh
  • Ingram, Lonnie O.
  • Shanmugam, K. T..
http://linked.open...ain/vavai/riv/wos
  • 000268308000005
http://linked.open...n/vavai/riv/zamer
issn
  • 0273-2289
number of pages
http://localhost/t...ganizacniJednotka
  • 11310
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 48 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software