Characterization and purification of a hydrogenase from the eukaryotic green alga Scenedesmus obliquus
Several catalytic properties of the hydrogenase from Scenedesmus obliquus have been examined to optimize the purification conditions. The K m -value for H 2-evolution in the presence of the most effective electron mediator methylviologen is 0.66 mM. The pH-optimum is 6.3, the temperature-optimum is...
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| Veröffentlicht in: | FEBS letters 1993-07, Vol.327 (1), p.21-24 |
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| creator | Schnackenberg, J. Schulz, R. Senger, H. |
| description | Several catalytic properties of the hydrogenase from
Scenedesmus obliquus have been examined to optimize the purification conditions. The
K
m
-value for H
2-evolution in the presence of the most effective electron mediator methylviologen is 0.66 mM. The pH-optimum is 6.3, the temperature-optimum is 50°C and the energy of activation is 38.4 ± 2 kJ·mol
−1. The soluble hydrogenase from the green alga,
Scenedesmus obliquus, was purified 1290-fold to homogeneity. The enzyme consists of two subunits with molecular masses of 55 kDa and 36 kDa. The molecular weight of the native enzyme, determined by gel filtration, is 150 ± 5 kDa. |
| doi_str_mv | 10.1016/0014-5793(93)81030-4 |
| format | Article |
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Scenedesmus obliquus have been examined to optimize the purification conditions. The
K
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-value for H
2-evolution in the presence of the most effective electron mediator methylviologen is 0.66 mM. The pH-optimum is 6.3, the temperature-optimum is 50°C and the energy of activation is 38.4 ± 2 kJ·mol
−1. The soluble hydrogenase from the green alga,
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Scenedesmus obliquus have been examined to optimize the purification conditions. The
K
m
-value for H
2-evolution in the presence of the most effective electron mediator methylviologen is 0.66 mM. The pH-optimum is 6.3, the temperature-optimum is 50°C and the energy of activation is 38.4 ± 2 kJ·mol
−1. The soluble hydrogenase from the green alga,
Scenedesmus obliquus, was purified 1290-fold to homogeneity. The enzyme consists of two subunits with molecular masses of 55 kDa and 36 kDa. The molecular weight of the native enzyme, determined by gel filtration, is 150 ± 5 kDa.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chlorophyta - enzymology</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors</subject><subject>Enzyme Stability</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Eukaryotic Cells - enzymology</subject><subject>Eukaryotic hydrogenase</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrogenase - analysis</subject><subject>Hydrogenase - isolation & purification</subject><subject>Molecular Weight</subject><subject>Oxidoreductases</subject><subject>Scenedesmus obliquus</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU2P0zAQhi0EWsrCPwDJB4SWQ8BfSZwLElRbQFqJA3C2Js64NaRx105A3V-Ps6l6BCRLlmeeecfzDiHPOXvDGa_eMsZVUdaNvGrka82ZZIV6QFZc17KQqtIPyeqMPCZPUvrB8lvz5oJcaClL1rAVcesdRLAjRn8How8DhaGjhyl65-0SCI4C3R27GLY4QELqYtjTcYcUp58Qj2H0lm4jYq7tt0C_Whyww7SfEg1t72-nKT0ljxz0CZ-d7kvyfXP9bf2puPny8fP6_U1hS1GpQkmntADZ1a6TpbUaRe3aFqCzla6sKDlyKFGxVtQ1b7G2SjSuyWOVAhQHeUleLbqHGG4nTKPZ-2Sx72HAMCVTl1oKptk_QV5VjZa8zqBaQBtDShGdOUS_z2Mbzsy8BzObbGaTTT73ezAql7046U_tHrtz0cn4nH95ykOy0LsIg_XpjCktS1WJjG0W7Lfv8fhfrc3m-oOYE3O8kffR-T_vFiHM7v_yGE2yHgeLnY9oR9MF__eB_gCid7gg</recordid><startdate>19930719</startdate><enddate>19930719</enddate><creator>Schnackenberg, J.</creator><creator>Schulz, R.</creator><creator>Senger, H.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19930719</creationdate><title>Characterization and purification of a hydrogenase from the eukaryotic green alga Scenedesmus obliquus</title><author>Schnackenberg, J. ; Schulz, R. ; Senger, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5264-43f482a3d7fd35cc8e27fbbaadc686c251e1a5e40b2771be7c429f900152a41a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chlorophyta - enzymology</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activation</topic><topic>Enzyme Inhibitors</topic><topic>Enzyme Stability</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Eukaryotic Cells - enzymology</topic><topic>Eukaryotic hydrogenase</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. 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Scenedesmus obliquus have been examined to optimize the purification conditions. The
K
m
-value for H
2-evolution in the presence of the most effective electron mediator methylviologen is 0.66 mM. The pH-optimum is 6.3, the temperature-optimum is 50°C and the energy of activation is 38.4 ± 2 kJ·mol
−1. The soluble hydrogenase from the green alga,
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| fulltext | fulltext |
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| ispartof | FEBS letters, 1993-07, Vol.327 (1), p.21-24 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present); Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Chlorophyta - enzymology Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Enzyme Activation Enzyme Inhibitors Enzyme Stability Enzymes and enzyme inhibitors Eukaryotic Cells - enzymology Eukaryotic hydrogenase Freshwater Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrogenase - analysis Hydrogenase - isolation & purification Molecular Weight Oxidoreductases Scenedesmus obliquus Substrate Specificity Temperature |
| title | Characterization and purification of a hydrogenase from the eukaryotic green alga Scenedesmus obliquus |
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