Flavin properties

The second step involves the transfer of electrons from the reduced [FMNHg] to a series of Fe-S proteins, including both 2Fe-2S and 4Fe-4S clusters (see Figures 20.8 and 20.16). The unique redox properties of the flavin group of FMN are probably important here. NADH is a two-electron donor, whereas the Fe-S proteins are one-electron transfer agents. The flavin of FMN has three redox states—the oxidized, semiquinone, and reduced states. It can act as either a one-electron or a two-electron transfer agent and may serve as a critical link between NADH and the Fe-S proteins. 

Hastings, J. W., Balny, C., Le Peuch, C., and Douzou, P. (1973). Spectral properties of an oxygenated luciferase-flavin intermediate isolated by low-temperature chromatography. Proc. Natl. Acad. Sci. USA 70 3468-3472. 

Tu, S.-C. (1979). Isolation and properties of bacterial luciferase-oxygenated flavin intermediate complexed with long-chain alcohols. Biochemistry 18 5940-5945. 

Riboflavin is heat-stable in the absence of light, but extremely photosensitive. It has a high degree of natural fluorescence when excited by UV light. This property can be used for detection and determination. Two coenzymes (Fig. 2), flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), are derived from riboflavin. 

Valle, L. Moran Vieyra, F.E. Borsarelli, C.D. (2011). Microenvironmental modulation of photophysical properties of flavins. Submitted to Photophysical and Photochemical Sciences. 

The addition of sulfite to APS reductase results in changes of the flavin visible spectrum that are explained by the formation of an adduct between the sulfite and the FAD group (135). Addition of AMP to the as-isolated enzyme causes no change in the spectroscopic properties. Addition of AMP to the sulfite-reacted enzyme causes the reduction of center I. However, the formation of a semiquinone signal has never been observed either by EPR or visible spectroscopies. Also, Mossbauer and EPR data indicate that AMP closely interacts with center I (139). 

Eppink MHM, SA Boeren, J Vervoort, WJH van Berkel (1997) Purification and properties of 4-hydroxyben-zoate 1-hydroxylase (decarboxylating), a novel flavin adenein dinucleotide-dependent monooxygenase from Candida parapilosis CBS604. J Bacteriol 179 6680-6687. 

Chen YP, DE Lincol, SA Woodin, CR Lovell (1991) Purification and properties of a unique flavin-containing chloroperoxidase from the capitellid polychaete Notomastus lobatus. J Biol Chem 266 23909-23915. 

Under conditions of copper deficiency, some methanotrophs can express a cytosolic, soluble form of MMO (sMMO) (20-23), the properties of which form the focus of the present review. The sMMO system comprises three separate protein components which have all been purified to homogeneity (24,25). The hydroxylase component, a 251 kD protein, contains two copies each of three subunits in an a 82y2 configuration. The a subunit of the hydroxylase houses the dinuclear iron center (26) responsible for dioxygen activation and for substrate hydroxylation (27). The 38.6 kD reductase contains flavin adenine dinucleotide (FAD) and Fe2S2 cofactors (28), which enable it to relay electrons from reduced nicotinamide adenine dinucleotide (NADH) to the diiron center in the... 

Whatever the reason may be behind the strict necessity to deprotonate the flavin donor, the reduced and deprotonated flavin was established in these model studies to be an efficient electron donor, able to reduce nucle-obases and oxetanes. In the model compounds 1 and 2 the pyrimidine dimer translates the electron transfer step into a rapidly detectable chemical cycloreversion reaction [47, 48], Incorporation of a flavin and of a cyclobutane pyrimidine dimer into DNA double strands was consequently performed in order to analyse the reductive electron transfer properties of DNA. 

Voropai ES, Samtsov MP, Kaplevskii KN, Maskevich AA, Stepuro VI, Povarova OI, Kuznetsova IM, Turoverov KK, Fink AL, Uverskii VN (2003) Spectral properties of thio-flavin T and its complexes with amyloid fibrils. J Appl Spectrosc 70(6) 868-874... 

The acidobasic properties of the flavin triplet are changed dramatically upon... 

Among the many sensory reactions Phycomyces displays, the study of the photoreceptor and adaptation deserves maximal attention, since Phycomyces shares these two attributes with a variety of other blue light sensitive organisms. Action-spectroscopy indicates a flavin as the photoreceptor of Phycomyces. /3-carotene was positively ruled out as a possible receptor, since mutants with no trace amounts of )3-carotene are phototropical normal. The photoreceptor has not yet been isolated. As in other systems the difficulty consists in distinguishing the flavin photoreceptor from the bulk flavoproteins in the cell. One therefore needs unambiguous criteria for the identification of the photoreceptor. The most promising approach for an isolation would be a photoreceptor mutant and we described the properties those mutants should have. Until now there is no firm evidence that the photomutants, madA or madB are defective in the photoreceptor. 

The cytochrome b and flavin content and properties of the 02 -forming NADPH oxidase solubilized from activated neutrophils. Biochim. Biophys. Acta 746, 40-7. 

Upon purification of the XDH from C. purinolyticum, a separate Se-labeled peak appeared eluting from a DEAE sepharose column. This second peak also appeared to contain a flavin based on UV-visible spectrum. This peak did not use xanthine as a substrate for the reduction of artificial electron acceptors (2,6 dichlor-oindophenol, DCIP), and based on this altered specificity this fraction was further studied. Subsequent purification and analysis showed the enzyme complex consisted of four subunits, and contained molybdenum, iron selenium, and FAD. The most unique property of this enzyme lies in its substrate specificity. Purine, hypoxanthine (6-OH purine), and 2-OH purine were all found to serve as reductants in the presence of DCIP, yet xanthine was not a substrate at any concentration tested. The enzyme was named purine hydroxylase to differentiate it from similar enzymes that use xanthine as a substrate. To date, this is the only enzyme in the molybdenum hydroxylase family (including aldehyde oxidoreductases) that does not hydroxylate the 8-position of the purine ring. This unique substrate specificity, coupled with the studies of Andreesen on purine fermentation pathways, suggests that xanthine is the key intermediate that is broken down in a selenium-dependent purine fermentation pathway. ... 

---