Biological Chemistry - Berezov T. T., Korovkin B. F. 1998

Chemistry of Conjugated Proteins
Chromoproteins
Flavoproteins

Flavoproteins contain protein-bound prosthetic groups derived from isoalloxazine, specifically oxidized flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). Flavoproteins are components of oxidoreductases, which are Enzymes that catalyze redox reactions within The Cell. Some flavoproteins also contain Metal Ions. Typical representatives of flavoproteins that also contain non-heme iron include xanthine oxidase, aldehyde oxidase, SDH, dihydroorotate dehydrogenase, acyl-CoA dehydrogenase, and electron-transferring flavoprotein. The latter two account for up to 80% of mitochondrial flavoproteins, which play a crucial role in cellular Bioenergetics (see Chapter 9). Non-heme iron binds to a protein component distinct from heme-containing chromoproteins. The iron is covalently linked to the sulfur atom of a Cysteine residue within the protein. Acid Hydrolysis of such Proteins releases iron and H2S. Despite structural differences from Cytochromes, non-heme flavoproteins perform a similar function in electron transport due to their ability to transition between oxidized and reduced states.



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