Flavin redox switching of protein functions

• Published in: Antioxidants & redox signaling Vol. 14; no. 6; p. 1079
• Main Authors: Becker, Donald F, Zhu, Weidong, Moxley, Michael A
• Format: Journal Article
• Language: English
• Published: United States 15-03-2011
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Flavins - metabolism; Flavoproteins - chemistry; Flavoproteins - metabolism; Fungal Proteins - chemistry; Fungal Proteins - metabolism; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Oxidation-Reduction; Protein Structure, Secondary; Pyruvate Oxidase - chemistry; Pyruvate Oxidase - metabolism
• ISSN: 1557-7716
• DOI: 10.1089/ars.2010.3417

Flavin cofactors impart remarkable catalytic diversity to enzymes, enabling them to participate in a broad array of biological processes. The properties of flavins also provide proteins with a versatile redox sensor that can be utilized for converting physiological signals such as cellular metabolism, light, and redox status into a unique functional output. The control of protein functions by the flavin redox state is important for transcriptional regulation, cell signaling pathways, and environmental adaptation. A significant number of proteins that have flavin redox switches are found in the Per-Arnt-Sim (PAS) domain family and include flavoproteins that act as photosensors and respond to changes in cellular redox conditions. Biochemical and structural studies of PAS domain flavoproteins have revealed key insights into how flavin redox changes are propagated to the surface of the protein and translated into a new functional output such as the binding of a target protein in a signaling pathway. Mechanistic details of proteins unrelated to the PAS domain are also emerging and provide novel examples of how the flavin redox state governs protein-membrane interactions in response to appropriate stimuli. Analysis of different flavin switch proteins reveals shared mechanistic themes for the regulation of protein structure and function by flavins.