Characterization of oxidative phosphorylation enzymes in Euglena gracilis and its white mutant strain W(gm)ZOflL
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25660326
DOI
10.1016/j.febslet.2015.01.035
PII: S0014-5793(15)00064-2
Knihovny.cz E-zdroje
- Klíčová slova
- Bleaching, Euglenozoa, Mitochondria, Respiratory chain, Trypanosomatids,
- MeSH
- elektronový transportní řetězec chemie metabolismus MeSH
- Euglena gracilis enzymologie genetika MeSH
- mitochondrie enzymologie MeSH
- mutace MeSH
- oxidativní fosforylace * MeSH
- protozoální proteiny chemie metabolismus MeSH
- spotřeba kyslíku MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- elektronový transportní řetězec MeSH
- protozoální proteiny MeSH
The enzymes involved in Euglena oxidative phosphorylation (OXPHOS) were characterized in this study. We have demonstrated that Euglena gracilis strain Z and its stable bleached non-photosynthetic mutant strain WgmZOflL both possess fully functional OXPHOS apparatus as well as pathways requiring terminal alternative oxidase(s) and alternative mitochondrial NADH-dehydrogenase(s). Light (or dark) and plastid (non)functionality seem to have little effect on oxygen consumption, the activities of the enzymes involved in OXPHOS and the action of respiration inhibitors in Euglena. This study also demonstrates biochemical properties of complex III (cytochrome c reductase) in Euglena.
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