Properties of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum

The nitrate reductase of the hyperthermophilic archaeon Pyrobaculum aerophilum was purified 137-fold from the cytoplasmic membrane. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, the enzyme complex consists of three subunits with apparent molecular weights of 130,000, 5...

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Vydané v:	Journal of bacteriology Ročník 183; číslo 19; s. 5491
Hlavní autori:	Afshar, S, Johnson, E, de Vries, S, Schröder, I
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 01.10.2001
Predmet:	Enzyme Stability Hydrogen-Ion Concentration Kinetics Molecular Weight Molybdoferredoxin Nitrate Reductase Nitrate Reductases - chemistry Nitrate Reductases - isolation & purification Nitrate Reductases - metabolism Protein Subunits Temperature Thermoproteaceae - enzymology
ISSN:	0021-9193
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