Abstract
Publisher Summary This chapter analyzes effect of conformation on the binding of flavins to flavoenzymes. The interaction of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) with specific proteins confers a great degree of versatility to these coenzymes as evidenced by the wide variety of reactions catalyzed by flavoproteins. An examination of the detailed tabulation of flavoproteins compiled by Palmer and Massey reveals the diversity of reactions catalyzed by these enzymes. A large number of flavoproteins effect the transfer of electrons between a donor and an acceptor; displaying considerable specificity for the former and much less for the latter. A smaller group of flavoenzymes serve as mixed function oxygenases. In addition, FAD and FMN are also members of multicomponent electron transfer systems such as those present in the metalloflavoproteins and respiratory chain-linked dehydrogenases. The functional diversity of these enzymes must to a large extent reside in the interactions between the flavocoenzyme and the protein matrices. In this chapter, basic concepts related to nature of binding are presented. Effect on flavin absorption spectrum is elaborated. Properties of apoflavoproteins are also described.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
