Cytochromes P450 in nanodiscs.
Nanodiscs have proven to be a versatile tool for the study all types of membrane proteins, including receptors, transporters, enzymes and viral antigens. The self-assembled Nanodisc system provides a robust and common means for rendering these targets soluble in aqueous media while providing a native like bilayer environment that maintains functional activity. This system has thus provided a means for studying the extensive collection of membrane bound cytochromes P450 with the same biochemical and biophysical tools that have been previously limited to use with the soluble P450s. These include a plethora of spectroscopic, kinetic and surface based methods. Significant improvements in homogeneity and stability of these preparations open new possibilities for detailed analysis of equilibrium and steady-state kinetic characteristics of catalytic mechanisms of human cytochromes P450 involved in xenobiotic metabolism and in steroid biosynthesis. The experimental methods developed for physico-chemical and functional studies of membrane cytochromes P450 incorporated in Nanodiscs allow for more detailed understanding of the scientific questions along the lines pioneered by Professor Klaus Ruckpaul and his array of colleagues and collaborators.
Denisov
Ilia G
IG
Department of Biochemistry, School of Molecular and Cellular Biology, The University of Illinois, 505 South Goodwin Avenue Urbana, IL 61801, USA.
Sligar
Stephen G
SG
D055162:Biocatalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D049329:Nanostructures / Q000737:chemistry*; D012995:Solubility; D013053:Spectrophotometry; D013379:Substrate Specificity
D008051:Lipid Bilayers; D008565:Membrane Proteins; D003577:Cytochrome P-450 Enzyme System