Abstract
Most of the bacterial cytochrome P450 s require two kinds of electron transfer proteins, ferredoxin and ferredoxin reductase, and thus P450 s do not show catalytic activity by themselves. A microbial transglutaminase-mediated site-specific cross-linking enables the formation of fusion P450 protein with a branched structure, which is generated from a genetic fusion protein of P450–ferredoxin reductase and ferredoxin, an interactive nanoscale protein structure. This fusion P450 system is self-sufficient due to intramolecular electron transfer, which means the system does not require additional electron-transferring proteins. Because some components of bacterial cytochrome P450 system are interchangeable, this self-sufficient system can be applied to non-natural combination of P450 and electron transfer proteins from different species of bacteria.
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Acknowledgments
We are grateful to Ajimonoto Co. Inc. for providing the TGase sample.
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Hirakawa, H., Nagamune, T. (2011). Nanoscale-Engineered Cytochrome P450 System with a Branch Structure. In: Wang, P. (eds) Nanoscale Biocatalysis. Methods in Molecular Biology, vol 743. Humana Press. https://doi.org/10.1007/978-1-61779-132-1_1
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DOI: https://doi.org/10.1007/978-1-61779-132-1_1
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