Characterization of oxidative phosphorylation enzymes in Euglena gracilis and its white mutant strain W(gm)ZOflL
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25660326
DOI
10.1016/j.febslet.2015.01.035
PII: S0014-5793(15)00064-2
Knihovny.cz E-resources
- Keywords
- Bleaching, Euglenozoa, Mitochondria, Respiratory chain, Trypanosomatids,
- MeSH
- Electron Transport Chain Complex Proteins chemistry metabolism MeSH
- Euglena gracilis enzymology genetics MeSH
- Mitochondria enzymology MeSH
- Mutation MeSH
- Oxidative Phosphorylation * MeSH
- Protozoan Proteins chemistry metabolism MeSH
- Oxygen Consumption MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Electron Transport Chain Complex Proteins MeSH
- Protozoan Proteins 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.
References provided by Crossref.org
Unexpectedly Streamlined Mitochondrial Genome of the Euglenozoan Euglena gracilis
