Cytochrome c reductase belongs to a family of enzymes called oxidoreductases which catalyze the shuttling of electrons from one molecule to another. Specifically, cytochrome c reductase functions to transfer electrons between nicotinamide adenine dinucleotide (NAD) cofactors and cytochrome C protein acceptor molecules.
Structurally, cytochrome c reductase is a flavoprotein, which means it contains a nucleic acid derivative of riboflavin as a vital component of the enzyme structure. Termed flavin dinucleotide, this region is critical for shuttling the electrons between NAD and cytochrome c and is key for forming ATP.
Cytochrome c is a small protein which contains an iron ring structure (heme) as part of the molecule. It is critically tied to complexes which carry out the electron transport chain and cellular respiration within the mitochondria.
In addition to various types of electron transport chain research studies, cytochrome c reductase has been used in manufacturing biosensors for detecting nitrite.