Use of bioconjugation with cytochrome P450 enzymes |
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| Affiliation: | 1. Department of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA;2. Division of Metabolism, Endocrinology, and Diabetes, Department of Internal Medicine, Ann Arbor, MI 48019, USA;3. Department of Pharmacology, University of Michigan, Ann Arbor, MI 48019, USA;1. Polyclinique de Courlancy, 38 bis rue de Courlancy, 51100 Reims, France;2. Service d’urologie et chirurgie de la transplantation, hôpital Edouard-Herriot, 5 place d’Arsonval, 69437 Lyon Cedex 03, France;3. Département d’urologie, CHU Saint-Louis, AP-HP, Paris Inserm U955Eq7, Paris-Est Créteil, France;4. CHU Mondor, AP-HP, Inserm U955Eq07, 51 avenue du Maréchal-de-Lattre-de-Tassigny, 94000 Créteil, France;5. Service d’urologie, CHU de Bordeaux, université Bordeaux-Segalen, 33000 Bordeaux, France;1. Institute of Biomedical Chemistry, 119121 Moscow, Russia;2. N.I. Pirogov Russian National Research Medical University, 117997 Moscow, Russia |
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| Abstract: | Bioconjugation, defined as chemical modification of biomolecules, is widely employed in biological and biophysical studies. It can expand functional diversity and enable applications ranging from biocatalysis, biosensing and even therapy. This review summarizes how chemical modifications of cytochrome P450 enzymes (P450s or CYPs) have contributed to improving our understanding of these enzymes. Genetic modifications of P450s have also proven very useful but are not covered in this review. Bioconjugation has served to gain structural information and investigate the mechanism of P450s via photoaffinity labeling, mechanism-based inhibition (MBI) and fluorescence studies. P450 surface acetylation and protein cross-linking have contributed to the investigation of protein complexes formation involving P450 and its redox partner or other P450 enzymes. Finally, covalent immobilization on polymer surfaces or electrodes has benefited the areas of biocatalysis and biosensor design. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone. |
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