Homology modeling of cytochrome P450scc and the mutations for optimal amperometric sensor.
A new homology model of bovine cytochrome P450scc is obtained starting from the recently determined crystal structure of mammalian cytochrome P450 2B4. The new emerging structure appears compatible with recent diffraction patterns of bovine P450scc microcrystals as obtained at the Microfocus Beamline of the European Synchrotron Radiation in Grenoble and here reported for the first time. The same atomic structure is utilized thereby to predict the mutations needed for modifying redox potential. A comprehensive comparison is finally carried out with the previous model present in the RCSB Protein DataBank also in terms of the alternative mutations being predicted for the same functional modification. The implication of these studies for optimal sensor construction is discussed.
Sivozhelezov
Victor
V
Fondazione Elba, Via delle Testuggini snc, 00100 Rome, Italy.
Nicolini
Claudio
C
D000818:Animals; D002417:Cattle; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000235:genetics*; D018360:Crystallography, X-Ray; D004594:Electrophysiology; D008957:Models, Genetic; D009154:Mutation; D010084:Oxidation-Reduction; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013329:Structure-Activity Relationship
D002786:Cholesterol Side-Chain Cleavage Enzyme