Characterization of the transient fluorescence wave phenomenon that occurs during H2 production in Chlamydomonas reinhardtii

Electron transport, mediated by NDA2 in H2-producing C. reinhardtii cells, shifts redox equilibria between the plastoquinone pool and PSII, and is observed as a transient fluorescence wave after a single flash.

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Characterization of cell growth and photobiological H2 production of Chlamydomonas reinhardtii in ASSF industry wastewater

International Journal of Hydrogen Energy ◽

10.1016/j.ijhydene.2014.03.132 ◽

2014 ◽

Vol 39 (25) ◽

pp. 13462-13467 ◽

Cited By ~ 10

Author(s):

Ming Chen ◽

Lei Zhang ◽

Shizhong Li ◽

Sandra Chang ◽

Wenrui Wang ◽

...

Keyword(s):

Cell Growth ◽

Chlamydomonas Reinhardtii ◽

H2 Production ◽

Photobiological H2 Production ◽

Industry Wastewater

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Characterization of atpA and atpB deletion mutants produced in Chlamydomonas reinhardtii cw15: electron transport and photophosphorylation activities of isolated thylakoids

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/s0005-2728(96)00123-5 ◽

1997 ◽

Vol 1319 (1) ◽

pp. 109-118 ◽

Cited By ~ 9

Author(s):

Heike R Fiedler ◽

Jacob Schlesinger ◽

Heinrich Strotmann ◽

Noun Shavit ◽

Stefan Leu

Keyword(s):

Electron Transport ◽

Chlamydomonas Reinhardtii ◽

Deletion Mutants

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Characterization of an Electron Transport Pathway Associated with Glucose and Fructose Respiration in the Intact Chloroplasts of Chlamydomonas reinhardtii and Spinach

PLANT PHYSIOLOGY ◽

10.1104/pp.100.1.327 ◽

1992 ◽

Vol 100 (1) ◽

pp. 327-333 ◽

Cited By ~ 9

Author(s):

Kausal K. Singh ◽

Changguo Chen ◽

Martin Gibbs

Keyword(s):

Electron Transport ◽

Chlamydomonas Reinhardtii ◽

Transport Pathway ◽

Intact Chloroplasts ◽

Electron Transport Pathway

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Faculty Opinions recommendation of Identification and characterization of an assembly intermediate subcomplex of photosystem I in the green alga Chlamydomonas reinhardtii.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.3256956.2952058 ◽

2010 ◽

Author(s):

Nathan Nelson ◽

Alexey Amunts

Keyword(s):

Chlamydomonas Reinhardtii ◽

Green Alga ◽

Photosystem I ◽

Assembly Intermediate ◽

Identification And Characterization

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An Improved Top-Down Mass Spectrometry Characterization of Chlamydomonas reinhardtii Histones and Their Post-translational Modifications

Journal of the American Society for Mass Spectrometry ◽

10.1021/jasms.1c00029 ◽

2021 ◽

Author(s):

Sarah R. Rommelfanger ◽

Mowei Zhou ◽

Henna Shaghasi ◽

Shin-Cheng Tzeng ◽

Bradley S. Evans ◽

...

Keyword(s):

Mass Spectrometry ◽

Chlamydomonas Reinhardtii ◽

Top Down ◽

Post Translational Modifications ◽

Top Down Mass Spectrometry

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Mutants of Chlamydomonas reinhardtii Deficient in Mitochondrial Complex I: Characterization of Two Mutations Affecting the nd1 Coding Sequence

Genetics ◽

10.1093/genetics/158.3.1051 ◽

2001 ◽

Vol 158 (3) ◽

pp. 1051-1060

Author(s):

Claire Remacle ◽

Denis Baurain ◽

Pierre Cardol ◽

René F Matagne

Keyword(s):

Mitochondrial Genome ◽

Chlamydomonas Reinhardtii ◽

Complex I ◽

Slow Growth ◽

Nadh:Ubiquinone Oxidoreductase ◽

Sequencing Analysis ◽

Mitochondrial Complex ◽

Genetical Analysis ◽

Complex I Activity

Abstract The mitochondrial rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) comprises more than 30 subunits, the majority of which are encoded by the nucleus. In Chlamydomonas reinhardtii, only five components of complex I are coded for by mitochondrial genes. Three mutants deprived of complex I activity and displaying slow growth in the dark were isolated after mutagenic treatment with acriflavine. A genetical analysis demonstrated that two mutations (dum20 and dum25) affect the mitochondrial genome whereas the third mutation (dn26) is of nuclear origin. Recombinational analyses showed that dum20 and dum25 are closely linked on the genetic map of the mitochondrial genome and could affect the nd1 gene. A sequencing analysis confirmed this conclusion: dum20 is a deletion of one T at codon 243 of nd1; dum25 corresponds to a 6-bp deletion that eliminates two amino acids located in a very conserved hydrophilic segment of the protein.

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