Regular ArticleRecombinant Human Cytochrome P450 1A2 and an N-Terminal-Truncated Form: Construction, Purification, Aggregation Properties, and Interactions with Flavodoxin, Ferredoxin, and NADPH-Cytochrome P450 Reductase
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Solar-powered P450 catalysis: Engineering electron transfer pathways from photosynthesis to P450s
2023, Journal of Inorganic BiochemistryA large-scale comparative analysis of affinity, thermodynamics and functional characteristics of interactions of twelve cytochrome P450 isoforms and their redox partners
2019, BiochimieCitation Excerpt :The positive ΔH values of CYP/CPR complexes might be associated with the disruption of intramolecular hydrogen bonds and salt bridges occurring upon reductase conformational changes. In addition to conformational rearrangements, hydrophobic interactions between CYP and CPR membrane domains contribute to the entropy component ΔG [6,23,50]. In this work, we used truncated CYP19A1 and CYP21A2 lacking the membrane-anchoring domain.
Characterization of Cytochrome P450 Enzymes and Their Applications in Synthetic Biology
2018, Methods in EnzymologyCitation Excerpt :In the absence of a native redox partner system, exogenous redox partner systems should be investigated. For instance, spinach ferredoxin/ferredoxin reductase, which are commercially available, or, e.g., E. coli flavodoxin (FLD)/FLDR are often used as nonnative redox partners (Dong, Yamazaki, Guo, & Guengerich, 1996; Jenkins & Waterman, 1994). It is also routine to test a number of different stoichiometries of redox partners in order to identify the best turnover conditions, and possibly to use both an iron–sulfur cluster-containing ferredoxin and a FMN-containing flavodoxin to establish which is preferred as the redox partner.
Display of membrane proteins on the heterologous caveolae carved by caveolin-1 in the Escherichia coli cytoplasm
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2014, Journal of Biological ChemistryFormation of P450 • P450 complexes and their effect on P450 function
2012, Pharmacology and TherapeuticsCitation Excerpt :Subsequently, truncated P450 enzymes were expressed without the N-terminal sequence. Despite the absence of the respective N-terminal sequences, it was found that CYP2E1 (Pernecky et al., 1993), CYP2B4 (Pernecky et al., 1995; Scott et al., 2001), CYP1A2 (Dong et al., 1996), and CYP2C3 (von Wachenfeldt et al., 1997) still tended to aggregate and associate with lipid membranes with little impairment of catalytic abilities. In the cases of CYP2E1, CYP2B4, and CYP1A2, the truncated enzymes formed aggregates that were as large as those associated with the wild type enzymes in the absence of detergent.