ArticleCurrent genetics2012
Characterization of an internal type-II NADH dehydrogenase from Chlamydomonas reinhardtii mitochondria.
Article in Current genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Inactivation of mitochondrial complex I stimulates chloroplast ATPase in Physcomitrium patens.Plant physiology · 2021Article
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- Insights into the respiratory chain and oxidative stress.Bioscience reports · 2018Review
- Mitochondria Affect Photosynthetic Electron Transport and Photosensitivity in a Green Alga.Plant physiology · 2018Article
- Impaired Mitochondrial Transcription Termination Disrupts the Stromal Redox Poise inPlant physiology · 2017Article
- A refined genome-scale reconstruction of Chlamydomonas metabolism provides a platform for systems-level analyses.The Plant journal : for cell and molecular biology · 2015Article
- The dual targeting ability of type II NAD(P)H dehydrogenases arose early in land plant evolution.BMC plant biology · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type-II NAD(P)H dehydrogenases form a multigene family that comprise six members in the green microalga Chlamydomonas. To date, only one enzyme (Nda2) located in the chloroplast has been characterized in this alga and demonstrated to participate in the reduction of the plastoquinone pool. We present here the functional characterization of Nda1. The enzyme is located on the inner face of the inner mitochondrial membrane. Its downregulation leads to a slight decrease of NADH:ferricyanide activity and of dark whole cell respiration. To determine whether the reduction of Nda1 combined with the lack of complex I would affect mitochondrial processes, double mutants affected in both Nda1 and complex I were isolated. Respiration and growth rates in heterotrophic conditions were significantly altered in the double mutants investigated, suggesting that Nda1 plays a role in the oxidation of matrix NADH in the absence of complex I.
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