Eukaryotic Expression of the Cytochrome c Oxidase Subunit I of Sitophilus zeamais and Its Interaction with Allyl Isothiocyanate

Linlin Jiang 1, Dan Zhang 1, Yue Li 1, Wei Chen 1, Weilin Shi 1, Hua Wu 1 2, Zhiqing Ma 1 2

PMID: 36757172 DOI: 10.1021/acs.jafc.2c08363

Abstract

Sitophilus zeamais Motschulsky (Coleoptera: Curculionidae) is a destructive pest of stored grains around the world. Allyl isothiocyanate (AITC) was shown to have good bioactivity in the control of S. zeamais. In this study, the interaction of AITC on cytochrome c oxidase core subunits I (COX I) and their binding mechanism were determined using spectroscopic, isothermal titration calorimetry and molecular docking techniques. The results indicate the binding constant (Ka) of AITC and COX I was 6.742 × 103 L/mol. Analysis of spectroscopic revealed that the binding of COX I to reduced Cyt c induced conformational changes of reduced Cyt c, while AITC could competitively bind and inhibit the activity of the COX I protein. Moreover, molecular docking results suggested a sulfur atom in the AITC structure could form a hydrogen bond having a length of 3.3 Å with the Gly- 27 of COX I.

Keywords: Isothermal titration calorimetry; Sitophilus zeamais; allyl isothiocyanate; cytochrome c oxidase core subunits I; eukaryotic expression.