Redox control of protein conformation in flavoproteins.
Flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are two flavin prosthetic groups utilized as the redox centers of various proteins. The conformations and chemical properties of these flavins can be affected by their redox states as well as by photoreactions. Thus, proteins containing flavin (flavoproteins) can function not only as redox enzymes, but also as signaling molecules by using the redox- and/or light-dependent changes of the flavin. Redox and light-dependent conformational changes of flavoproteins are critical to many biological signaling systems. In this review, we summarize the molecular mechanisms of the redox-dependent conformational changes of flavoproteins and discuss their relationship to signaling functions. The redox-dependent (or light-excited) changes of flavin and neighboring residues in proteins act as molecular "switches" that "turn on" various conformational changes in proteins, and can be classified into five types. On the basis of the present analysis, we recommend future directions in molecular structural research on flavoproteins and related proteins.
Senda
Toshiya
T
Biomedicinal Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan. toshiya-senda@aist.go.jp
Senda
Miki
M
Kimura
Shigenobu
S
Ishida
Tetsuo
T
D005415:Flavins / Q000378:metabolism; D005420:Flavoproteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011487:Protein Conformation
D005415:Flavins; D005420:Flavoproteins