How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II.

ABSTRACT: The membrane-bound complex II family of proteins is composed of enzymes that catalyze succinate and fumarate interconversion coupled with reduction or oxidation of quinones within the membrane domain. The majority of complex II enzymes are protein heterotetramers with the different subunits harboring a variety of redox centers. These redox centers are used to transfer electrons between the site of succinate-fumarate oxidation/reduction and the membrane domain harboring the quinone. A covalently bound FAD cofactor is present in the flavoprotein subunit, and the covalent flavin linkage is absolutely required to enable the enzyme to oxidize succinate. Assembly of the covalent flavin linkage in eukaryotic cells and many bacteria requires additional protein assembly factors. Here, we provide me

SUBMITTER: Maklashina E 

PROVIDER: S-EPMC9557727 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature