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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Dettagli Bibliografici

Pubblicato in:	J Bacteriol
Autori principali:	Afshar, Sepideh, Johnson, Eric, de Vries, Simon, Schröder, Imke
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	American Society for Microbiology (ASM) 2001
Soggetti:	Enzymes and Proteins
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC95438/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11544209/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JB.183.19.5491-5495.2001
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