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Probing the structure of the linker connecting the reductase and heme domains of cytochrome P450BM-3 using site-directed mutagenesis.
Cytochrome P450BM-3 is a catalytically self-sufficient fatty acid hydroxylase containing one equivalent each of heme, FMN, and FAD. The heme and flavins reside in separate domains connected by a linker peptide. In an earlier study (Govindaraj S, Poulos T, 1995, Biochemistry 34:11221-11226), we found...
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| Hoofdauteurs: | , |
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| Formaat: | Artigo |
| Taal: | Inglês |
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Cold Spring Harbor Laboratory Press
1996
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143464/ https://ncbi.nlm.nih.gov/pubmed/8819171 |
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