MIMG 101 Study Guide - Quiz Guide: Oxidoreductase, Coenzyme Q10, Phospholipid

• School: UCLA
• Department: Microbiology, Immunology, and Molecular Genetics
• Course: MIMG 101
• Professor: G U N S A L U S& B R A D L E Y

Document Summary

Succinate dehydrogenase has 4 subunits forming a membrane bound heterotetramer. The subunits are fda binding protein sdha, iron-sulfur cluster binding protein sdhb, membrane protein sdhc, and membrane protein sdhd. A and b are hydrophilic and atached to the cytoplasmic surface of the plasma membrane via interacions with the two hydrophobic integral membrane subunits, c and d. a contains the fad cofactor and the dicarboxylic acid binding site. Electrons from the oxidaion of succinate are transferred through the iron-sulphur protein, sdhb, to a quinone binding site located at the interface of the sdhb, sdhc and sdhd subunits. The sdhc and sdhd subunits each contain three transmembrane helices and anchor the complex to the membrane. A single heme b556 cofactor bridges the sdhc and sdhd subunits. The enire enzyme is organised into a trimeric supercomplex. [subunit composiion of succinate:quinone oxidoreductase secion: glycerol-3-phosphate dehydrogenase enzyme (aerobic) is a homodimeric enzyme associated with the cytoplasmic membrane through binding to negaively-charged phospholipids.