Chemistry 3393A/B Lecture Notes - Lecture 3: Deprotonation, Competitive Inhibition, Hmg-Coa Reductase

• School: Western University
• Department: Chemistry
• Course: Chemistry 3393A/B
• Professor: Felix Lee

Document Summary

This topic covers the following sections of the textbook: After studying this chapter, you should be able to do the following textbook questions: Chapter 3: 1 4, 6; chapter 7: 1 5, 7, 8. And these multiple-(cid:272)hoi(cid:272)e (cid:395)uestio(cid:374)s o(cid:374) the te(cid:454)t(cid:271)ook"s (cid:449)e(cid:271)site (http://global. oup. com/uk/orc/chemistry/patrick5e/): chapter 3: 1 3, 5 8; chapter 7: 1, 3 5, 8 10. The (cid:396)ate at (cid:449)hi(cid:272)h (cid:455)ou (cid:862)go o(cid:448)e(cid:396) the hill(cid:863) dete(cid:396)(cid:373)i(cid:374)es the ki(cid:374)eti(cid:272) pa(cid:396)a(cid:373)ete(cid:396). The a(cid:373)ou(cid:374)t of e(cid:374)e(cid:396)g(cid:455) fo(cid:396) activation (ea) is a the(cid:396)(cid:373)od(cid:455)(cid:374)a(cid:373)i(cid:272) pa(cid:396)a(cid:373)ete(cid:396). I(cid:374) the p(cid:396)ese(cid:374)(cid:272)e of a (cid:272)atal(cid:455)st, g does not change because the sta(cid:396)ti(cid:374)g poi(cid:374)t a(cid:374)d the e(cid:374)d poi(cid:374)t does (cid:374)ot (cid:272)ha(cid:374)ge. Thus g is a state fu(cid:374)(cid:272)tio(cid:374) since it does not change, neither does the equilibrium. The enzyme simply provides an alternate path (i. e. mechanism) to make the reaction faster, thereby affecting the kinetics. k = ae -ea/rt a(cid:374)d g = -rt ln(k) From the arrhenius equation, as ea decreases, k increases.