scholarly journals Characterization of the Kinetic, Regulatory, and Structural Properties of ADP-Glucose Pyrophosphorylase from Chlamydomonas reinhardtii

1994 ◽  
Vol 104 (4) ◽  
pp. 1287-1294 ◽  
Author(s):  
A. A. Iglesias ◽  
Yy. Charng ◽  
S. Ball ◽  
J. Preiss
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Structural Properties ◽  
Adp Glucose Pyrophosphorylase

scholarly journals Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of Chlamydomonas reinhardtii Glutaredoxin 2

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 803
Author(s):  
Thomas Roret ◽  
Bo Zhang ◽  
Anna Moseler ◽  
Tiphaine Dhalleine ◽  
Xing-Huang Gao ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Structural Properties ◽  
Active Site ◽  
Fluorescent Protein ◽  
Spectroscopic Characterization ◽  
Redox Activity ◽  
Structural Factors ◽  
Oxidoreductase Activity ◽  
Iron Sulfur

Glutaredoxins (GRXs) are thioredoxin superfamily members exhibiting thiol-disulfide oxidoreductase activity and/or iron-sulfur (Fe-S) cluster binding capacities. These properties are determined by specific structural factors. In this study, we examined the capacity of the class I Chlamydomonas reinhardtii GRX2 recombinant protein to catalyze both protein glutathionylation and deglutathionylation reactions using a redox sensitive fluorescent protein as a model protein substrate. We observed that the catalytic cysteine of the CPYC active site motif of GRX2 was sufficient for catalyzing both reactions in the presence of glutathione. Unexpectedly, spectroscopic characterization of the protein purified under anaerobiosis showed the presence of a [2Fe-2S] cluster despite having a presumably inadequate active site signature, based on past mutational analyses. The spectroscopic characterization of cysteine mutated variants together with modeling of the Fe–S cluster-bound GRX homodimer from the structure of an apo-GRX2 indicate the existence of an atypical Fe–S cluster environment and ligation mode. Overall, the results further delineate the biochemical and structural properties of conventional GRXs, pointing to the existence of multiple factors more complex than anticipated, sustaining the capacity of these proteins to bind Fe–S clusters.

Characterization of Structural Properties in High Reynolds Hydraulic Jump Based on CFD and Physical Modeling Approaches

2020 ◽  
Vol 146 (12) ◽  
pp. 04020079 ◽  
Author(s):  
Juan Francisco Macián-Pérez ◽  
Arnau Bayón ◽  
Rafael García-Bartual ◽  
P. Amparo López-Jiménez ◽  
Francisco José Vallés-Morán
Keyword(s):  
Structural Properties ◽  
Physical Modeling ◽  
Hydraulic Jump ◽  
Modeling Approaches ◽  
High Reynolds

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

Genetics ◽  
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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