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Antonini M, Ghisellini P, Paternolli C, et al. Electrochemical study of the interaction between cytochrome P450sccK201E and cholesterol. Talanta. 2004;62(5):945-50doi: 10.1016/j.talanta.2003.10.023.
Antonini, M., Ghisellini, P., Paternolli, C., & Nicolini, C. (2004). Electrochemical study of the interaction between cytochrome P450sccK201E and cholesterol. Talanta, 62(5), 945-50. https://doi.org/10.1016/j.talanta.2003.10.023
Antonini, Mirco, et al. "Electrochemical study of the interaction between cytochrome P450sccK201E and cholesterol." Talanta vol. 62,5 (2004): 945-50. doi: https://doi.org/10.1016/j.talanta.2003.10.023
Antonini M, Ghisellini P, Paternolli C, Nicolini C. Electrochemical study of the interaction between cytochrome P450sccK201E and cholesterol. Talanta. 2004 Apr 19;62(5):945-50. doi: 10.1016/j.talanta.2003.10.023. PMID: 18969384.
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Talanta. 2004 Apr 19;62(5):945-50. doi: 10.1016/j.talanta.2003.10.023.

Electrochemical study of the interaction between cytochrome P450sccK201E and cholesterol.

Talanta

Mirco Antonini, Paola Ghisellini, Cristina Paternolli, Claudio Nicolini

Affiliations

  1. Department of Biophysical M&O Sciences and Technologies, University of Genova, Corso Europa, 30 16132 Genova, Italy.

PMID: 18969384 DOI: 10.1016/j.talanta.2003.10.023

Abstract

Cytochrome P450sccK201E, mutated form of cytochrome P450scc native recombinant (P450sccNR), was employed to study the enzyme-substrate interaction. The detection of the cholesterol was performed by electrochemical method using cyclic voltammetry (CV) and chronoamperometry measurements. The biochemical analysis was realized to observe the electrochemical responses of the engineerized enzyme to three different forms of cholesterol: free, low-density lipoprotein (LDL) and high-density lipoproteins (HDL). Compared to cytochrome P450sccNR, the cytochrome P450sccK201E displays a different behavior in the interaction with the substrate detection. The results show that the engineerized enzyme can be utilized for the cholesterol detection in biosensor field.

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