TAILIEUCHUNG - Báo cáo khoa học: Deflavination and reconstitution of flavoproteins Tackling fold and function

Flavoproteins are ubiquitous redox proteins that are involved in many biological the majority of flavoproteins, the flavin cofactor is tightlybut noncovalently dissociation of flavoproteins into apo-proteinandflavinprostheticgroupyields valuable insights in flavoprotein folding, of the natural cofactorwithartificial flavins has proved tobe especially useful for the determination of the solvent acces-sibility, polarity, reaction stereochemistry and dynamic behaviour of flavoprotein active sites | Eur. J. Biochem. 270 4227-4242 2003 FEBS 2003 doi REVIEW ARTICLE Deflavination and reconstitution of flavoproteins Tackling fold and function Marco H. Hefti Jacques Vervoort and Willem J. H. van Berkel Laboratory of Biochemistry Wageningen University the Netherlands Flavoproteins are ubiquitous redox proteins that are involved in many biological processes. In the majority of flavoproteins the flavin cofactor is tightly but noncovalently bound. Revrrsible disoociation of ílej or joleilrs into apoprotein and flavin prosthetic group yields valuable insights in flavoprotein folding function and mechanism. Reiflacement of the natural cofactor with artificial flavins has proved to be especially useful for the determination of the solvent accessibility polarity reaction stereochemistry and dynamic behaviour of flavoprotein active sites. In hlto reiiew we summarize the advances made in the field of flavoprotein deflavination and reconstitution. Serana I pophistícated chromatographic procedures to either deflavinate or reconstitute the flavoprotein on a large scale are discussed. In a subset of flavoproteins the flavin cofactor is covalently attached to the polypeptide chain. Studíes Irom ribonavin-deficient expression systems and site-directed mutagenesis suggest that the flavinylation reaction is a post-translational rather than a cotranslational process. These oeneric approaches have also provided insight into the mechanism of covalent flavinylation and the rationale for this atypical protein modification. Keywords apoprotein deflavination FAD flavin flavo-enzyme flavoprotein FMN metal affinity chromatography reconstitution. Introduction Flavoproteins are ubiquitous proteins that use flavins as prosthetic groups. The omimion flavin oifactore are FMN and FAD which are synthesized in vivo from riboflavin vitamin B1 by the action of riboflavin kinase 1 2 and FAD synthetase 3 . The redox attive ijoalloxazine moi ty of the flavin cofactor may

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