Photosystem I from plants as a bacterial cytochrome P450 surrogate electron donor: terminal hydroxylation of branched hydrocarbon chains
| Autor: | Paul R. Ortiz de Montellano, Birger Lindberg Møller, Kenneth Jensen, Jonathan B. Johnston |
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| Rok vydání: | 2011 |
| Předmět: |
Stereochemistry
Bioengineering Electron donor Hydroxylation Photosystem I Applied Microbiology and Biotechnology Article Cofactor chemistry.chemical_compound Cytochrome P-450 Enzyme System Oxidoreductase Ferredoxin chemistry.chemical_classification Photosystem I Protein Complex biology Chemistry Cytochrome b6f complex Mycobacterium tuberculosis General Medicine Hydrocarbons Biochemistry Sunlight biology.protein NAD+ kinase NADP Biotechnology |
| Zdroj: | Biotechnology Letters. 34:239-245 |
| ISSN: | 1573-6776 0141-5492 |
| Popis: | The ability of cytochrome P450 enzymes to catalyze highly regio- and stereospecific hydroxylations makes them attractive alternatives to approaches based on chemical synthesis but they require expensive cofactors, e.g. NAD(P)H, which limits their commercial potential. Ferredoxin (Fdx) is a multifunctional electron carrier that in plants accepts electrons from photosystem I (PSI) and facilitates photoreduction of NADP(+) to NADPH mediated by ferredoxin-NAD(P)H oxidoreductase (FdR). In bacteria, the electron flow is reversed and Fdx accepts electrons from NADPH via FdR and serves as the direct electron donor to bacterial P450s. By combining the two systems, we demonstrate that irradiation of PSI can drive the activity of a bacterial P450, CYP124 from Mycobacterium tuberculosis. The substitution of the costly cofactor NADPH with sunlight illustrates the potential of the light-driven hydroxylation system for biotechnology applications. |
| Databáze: | OpenAIRE |
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