Flavins Analysis Service


Flavin is the common name for a group of organic  compounds based on pteridine, formed by the tricyclic heterocycle isoalloxazine.  The riboflavin (RF), vitamin B2, is an essential precursor of flavin  adenine dinucleotide (FAD) and flavin mononucleotide (FMN) co-enzymes. Another  compound of the flavin family is lumiflavin. The flavins have in  common the isoalloxazine ring system where the redox process occurs. The nature  of the group attached to the N-10, is the flavin members differentiation and  can influence the flavin adsorption orientation on the electrode surface, leaving  the active site more or less available. The redox process of the flavins is  thermodynamically reversible, irrespective of whether one or two electrons per  flavin molecule are being transferred, which means that their redox states  (quinone state, semiquinone state, hydroquinone state) must be considered.

Flavins analysis.  Figure  1. Chemical structure and nomenclature of the flavins in oxidized state (a) and  redox process of part of flavin structure (b).

Flavins  are useful in physiologic systems in that they are stronger oxidizing agents  than NAD+,  thus fitting in further along the electron transport chain. They participate in  one or two electron processes (and thus reactions with free radicals or metal  ions), and in reduced form react directly with O (as in hydroxylation reactions).  Riboflavin is thus an enzyme cofactor, or coenzyme, fundamental to many areas  of metabolism, and is intimately involved in processes by which the oxidation  of glucose and fatty acids are utilized for adenosine triphosphate (ATP)  formation, and thus the support of metabolic processes. Riboflavin coenzyme  formation (and thus trapping within cells), is initiated through  phosphorylation by a flavokinase, which is positively regulated by the most  active form of thyroid hormone.

Flavins  that are bound to proteins are resistant to degradation. However, unbound forms  are subject to catabolism. Both FAD and FMN are catabolized by intracellular  enzymes in ways directly analogous to the breakdown of these forms in foods  during their absorption across the intestinal mucosal cell. Thus, FAD is  converted to FMN by FAD-pyrophosphatase (releasing AMP), and FMN is degraded to  free riboflavin by FMN-phosphatases. Both FAD and FMN are split to yield free  riboflavin by alkaline phosphatase.

The  degradation of riboflavin per se involves initially its hydroxylation at the  7α- and 8α-positions of the isoalloxazine ring by hepatic microsomal cytochrome  P-450-dependent processes. It is thought that catabolism proceeds by the  oxidation and then removal of the methyl groups. The liver, in at least some  species, has the ability to form riboflavin α-glycosides. As a result of this  metabolism, human blood plasma contains FAD and FMN as the major riboflavin  metabolites, as well as small amounts of 7α-hydroxyriboflavin. Side chain  oxidation has been observed in bacterial systems, but not in higher animals.

Flavins analysis.  Figure  2. Riboflavin metabolism and cellular processing pathways.

The  chemistry of flavins has been studied extensively. Riboflavin is  a stable compound with a variety of interesting properties. FMN and FAD are  much more important in cells, but are less stable in solution because of the  presence of phosphate ester and anhydride bonds. Riboflavin is  responsible for the important biological chemistry of all flavins. One  reason that flavoproteins have been so extensively analyzed is that they  can be studied by examining the properties of their cofactor that is nearly  always involved in the core function of each protein. Another reason is the  variety of chemical properties that have been exploited for important  biological functions of considerable diversity.

Flavins  work as co-factors and form an integral part of the redox active sites of many  different enzymes involved in dehydrogenation reactions, dioxygen activation,  and electron transfer reactions. The understanding of the versatile chemistry  of flavins and the mechanisms of action of flavoprotein enzymes is of extreme  importance and has been focus of many investigations. Creative Proteomics  provides reliable, rapid and cost-effective flavins targeted flavins metabolomics  services.

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Flavins  Quantified in This Service

With  integrated set of separation, characterization, identification and  quantification systems featured with excellent robustness &  reproducibility, high and ultra-sensitivity, Creative Proteomics provides  reliable, rapid and cost-effective flavins targeted metabolomics services.

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