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- Isupov, Michail N., et al. Show all 6 Authors
- FEBS letters 2014 v.588 pp. 1616-1622
- Escherichia coli; Rhodobacteraceae; active sites; carbon; crystal structure; hydrophobicity
- ... A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A ...
- Isupov, Michail N., et al. Show all 9 Authors
- FEBS letters 2013 v.587 pp. 3633-3639
- crystal structure; cytochrome P-450; electron transfer; genes; horizontal gene transfer; humans; hydrophobicity; spectral analysis; transport proteins; viruses; yeasts
- ... Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytochrome b5 and additionally that the viral enzyme can substitute for yeast cytochrome b5 in yeast cytoc ...