Monovinyl and divinyl protochlorophyll in different stages of esterification isolated from mutant C-2A'of the unicellular green alga Scenedesmus obliquus

1994 ◽  
Vol 90 (3) ◽  
pp. 490-496 ◽  
Author(s):  
Rosemarie Knaust ◽  
Horst Senger
Keyword(s):  
Green Alga ◽  
Scenedesmus Obliquus ◽  
Unicellular Green Alga

Isolation and Purification to Apparent Homogeneity of 4,5-Dioxovalerate Aminotransferase from Scenedesmus obliquus Mutant C-2 A′

1988 ◽  
Vol 43 (7-8) ◽  
pp. 563-571 ◽  
Author(s):  
A. Kah ◽  
D. Dörnemann ◽  
H. Senger
Keyword(s):  
Molecular Weight ◽  
Green Alga ◽  
Isoelectric Point ◽  
Pyridoxal Phosphate ◽  
Scenedesmus Obliquus ◽  
Ph Optimum ◽  
Isolation And Purification ◽  
Apparent Homogeneity ◽  
Unicellular Green Alga ◽  
Glyoxylate Aminotransferase

In the present paper the purification of a specific 4,5-dioxovalerate transaminase from pigment mutant C-2 A′ of the unicellular green alga Scenedesmus obliquus to apparent homogeneity is described. The newly isolated enzyme ʟ-glutamate: 4,5-dioxovalerate aminotransferase is not identical with ʟ-alanine: 4,5-dioxovalerate aminotransferase (EC 2.6.1.43) and ʟ-alanine: glyoxylate aminotransferase (EC 2.6.1.44). A procedure for the purification is described and the resulting homogeneous protein is characterized by its Kᴍ-values for oxo-substrates and amino donors, its pyridoxal phosphate requirement, reversability of the catalysis, pH-optimum, isoelectric point and its molecular weight.

Purification and Characterization of Cytochrome c6 from the Unicellular Green Alga Scenedesmus obliquus

1997 ◽  
Vol 52 (11-12) ◽  
pp. 740-746 ◽  
Author(s):  
Röbbe Wünschiers ◽  
Thomas Zinn ◽  
Dietmar Linder ◽  
Rüdiger Schulz
Keyword(s):  
Cytochrome C ◽  
Green Alga ◽  
Scenedesmus Obliquus ◽  
Terminal Sequence ◽  
Ammonium Sulfate Precipitation ◽  
Purification And Characterization ◽  
Unicellular Green Alga ◽  
Sds Page ◽  
Monoraphidium Braunii

Abstract Purification of a soluble cytochrome c6 from the unicellular green alga Scenedesmus obliquus by a simple and rapid method is described. The purification procedure includes ammonium sulfate precipitation and non-denaturating PAGE. The N-terminal sequence of the first 20 amino acids was determined and shows 85% similarity and 75% identity to the sequence of cytochrome c6 from the green alga Monoraphidium braunii. The ferrocyto-chrome shows typical UV/VIS absorption peaks at 552.9, 521.9 and 415.7 nm. The apparent molecular mass was estimated to be 12 kD a by SDS-PAGE. EPR-spectroscopy at 20K shows resonances indicative for two distinct low-spin heme forms.

Kinetic Studies of Protochlorophyllide Reduction in vitro in the Greening Mutant C-2A' of the Unicellular Green Alga Scenedesmus obliquus

1995 ◽  
Vol 50 (11-12) ◽  
pp. 775-780 ◽  
Author(s):  
Thomas Urbig ◽  
Rosemarie K. C Knaust ◽  
Hilmar Schiller ◽  
Horst Sengera
Keyword(s):  
Green Alga ◽  
Ph Dependence ◽  
Strong Dependence ◽  
Scenedesmus Obliquus ◽  
Kinetic Studies ◽  
Unicellular Green Alga ◽  
Triggering Factor ◽  
Triton X

The NADPH-protochlorophyllide oxidoreductase, an enzyme catalysing the light-driven conversion of protochlorophyllide to chlorophyllide, was studied in the greening mutant C- 2A′ of the unicellular green alga Scenedesmus obliquus. Studies of the enzyme activity in vitro showed strong dependence on the presence of glycerol and the detergent Triton X-100. Prerequisite for the formation of a photoactive enzyme complex is a sufficient preincubation time with the substrates PChlide and NADPH. A continuous assay system, reading the absorbance increase at the wavelength of chlorophyllide, was used to determine the kinetic constants. The Km value for NADPH is 4.2 μᴍ, the Vmax is 5.9 pmol · s-1. The Km and Vmax for protochlorophyllide are 0.19 μᴍ and 6.5 pmol · s-1, respectively. The pH-dependence of the reaction exhibits a broad maximum between pH 7-8.5 typically for an enzyme active during chloroplast development, when pH-changes might be expected. The obtained kinetic data outline that the light dependent formation of chlorophyll in vivo is not limited by the substrates PChlide and NADPH, indicating that only light is the triggering factor in the very early greening process.

scholarly journals Bioenergetic Strategy for the Biodegradation of p-Cresol by the Unicellular Green Alga Scenedesmus obliquus

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e51852 ◽  
Author(s):  
Aikaterini Papazi ◽  
Konstantinos Assimakopoulos ◽  
Kiriakos Kotzabasis
Keyword(s):  
Green Alga ◽  
Scenedesmus Obliquus ◽  
Unicellular Green Alga

Bioenergetic reprogramming plasticity under nitrogen depletion by the unicellular green alga Scenedesmus obliquus

Planta ◽  
2017 ◽  
Vol 247 (3) ◽  
pp. 679-692 ◽  
Author(s):  
Aikaterini Papazi ◽  
Anna Korelidou ◽  
Efthimios Andronis ◽  
Athina Parasyri ◽  
Nikolaos Stamatis ◽  
...  
Keyword(s):  
Green Alga ◽  
Scenedesmus Obliquus ◽  
Nitrogen Depletion ◽  
Unicellular Green Alga

Evidence for Nickel in the Soluble Hydrogenase from the Unicellular Green Alga Scenedesmus obliquus

1994 ◽  
Vol 49 (1-2) ◽  
pp. 33-38 ◽  
Author(s):  
Thomas Zinn ◽  
Jörg Schnackenberg ◽  
Dieter Haak ◽  
Susanne Römer ◽  
Rüdiger Schulz ◽  
...  
Keyword(s):  
Green Alga ◽  
Dark Adaptation ◽  
Scenedesmus Obliquus ◽  
Gel Filtration ◽  
Final Concentration ◽  
Hydrogenase Activity ◽  
Adaptation Period ◽  
Unicellular Green Alga ◽  
Chelating Reagent ◽  
Parallel Fashion

Cultures of the green alga Scenedesmus obliquus were grown in the presence of either the chelating reagent EDTA or NiCl2 in various concentrations and assayed for hydrogenase catalyzed photohydrogen evolution after an anaerobic dark adaptation period. Cultivation of algae in the presence of 100 μm EDTA inhibited the formation of hydrogenase activity by 37%. After a cultivation of the cells in the presence of 5-20 μm NiCl2 photohydrogen evolution was increased by 20-40% . Addition of EDTA up to a final concentration of 1.5 mᴍ had no effect on the activity of hydrogenase in cell-free hydrogenase preparations. Cultures grown in the presence of radioactive 63NiCl2 incorporated 63Ni in a parallel fashion to the cell growth. In radioactive labeled hydrogenase preparations a co-elution of radioactivity and hydrogenase activity could be observed using gel filtration chromatography.

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