Coenzyme Q – cytochrome c reductaseThe coenzyme Q : cytochrome c – oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (), playing a critical role in biochemical generation of ATP (oxidative phosphorylation). Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits). Complex III is present in the mitochondria of all animals and all aerobic eukaryotes and the inner membranes of most eubacteria.
Lipid polymorphismPolymorphism in biophysics is the ability of lipids to aggregate in a variety of ways, giving rise to structures of different shapes, known as "phases". This can be in the form of spheres of lipid molecules (micelles), pairs of layers that face one another (lamellar phase, observed in biological systems as a lipid bilayer), a tubular arrangement (hexagonal), or various cubic phases (Fdm, Imm, Iam, Pnm, and Pmm being those discovered so far). More complicated aggregations have also been observed, such as rhombohedral, tetragonal and orthorhombic phases.
Heme AHeme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of heme B, a component of hemoglobin, the red pigment in blood. Heme A differs from heme B in that a methyl side chain at ring position 8 is oxidized to a formyl group and a hydroxyethylfarnesyl group, an isoprenoid chain, has been attached to the vinyl side chain at ring position 2 of the iron tetrapyrrole heme.
Acyl-CoA dehydrogenaseAcyl-CoA dehydrogenases (ACADs) are a class of enzymes that function to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells. Their action results in the introduction of a trans double-bond between C2 (α) and C3 (β) of the acyl-CoA thioester substrate. Flavin adenine dinucleotide (FAD) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function.
