Abstract
A new procedure for isolation of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens increasing significantly the yield of the purified enzyme is presented. The enzyme is isolated from the soluble fraction of the cell extract as a hexamer, as shown by gel filtration chromatography and small angle X-ray scattering analysis. Thermostability of the hexameric form of the nitrite reductase is characterized in terms of thermoinactivation and thermodenaturation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification*
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Chromatography, Gel
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Chromatography, Ion Exchange
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Cytochromes a1 / chemistry*
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Cytochromes a1 / isolation & purification*
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Cytochromes c1 / chemistry*
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Cytochromes c1 / isolation & purification*
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Ectothiorhodospiraceae / enzymology*
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Enzyme Stability
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Nitrate Reductases / chemistry*
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Nitrate Reductases / isolation & purification*
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Scattering, Small Angle
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Temperature
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X-Ray Diffraction
Substances
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Bacterial Proteins
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Cytochromes a1
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Cytochromes c1
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Nitrate Reductases
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nitrate reductase (cytochrome)