Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity.
Dimethyl sulfoxide reductase, a terminal electron transfer enzyme, was purified from anaerobically grown Escherichia coli harboring a plasmid which codes for dimethyl sulfoxide reductase. The enzyme was purified to greater than 90% homogeneity from cell envelopes by a three-step purification procedu...
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| Gepubliceerd in: | J Bacteriol |
|---|---|
| Hoofdauteurs: | , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
1988
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC210994/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3280546/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.170.4.1505-1510.1988 |
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