Deflavination and reconstitution of proteins. Tackling fold and function
| Autor: | Willem J. H. van Berkel, Marco H. Hefti, Jacques Vervoort |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
desulfovibrio-vulgaris flavodoxin
Flavoprotein Biochemie Flavin group environment and public health Biochemistry Cofactor chemistry.chemical_compound riboflavin-binding-protein flavin-adenine-dinucleotide Flavin adenine dinucleotide megasphaera-elsdenii flavodoxin p-hydroxybenzoate hydroxylase biology Butyryl-CoA dehydrogenase integumentary system EPS-1 apop Solvent accessibility butyryl-coa dehydrogenase amino-acid oxidase enzymes and coenzymes (carbohydrates) chemistry nuclear-magnetic-resonance Covalent bond biology.protein Protein folding active-site probes |
| Zdroj: | European Journal of Biochemistry, 270, 4227-4242 European Journal of Biochemistry 270 (2003) |
| ISSN: | 0014-2956 |
| DOI: | 10.1046/j.1432-1033.2003.03802.x |
| Popis: | 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. Reversible dissociation of flavoproteins into apoprotein and flavin prosthetic group yields valuable insights in flavoprotein folding, function and mechanism. Replacement 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 this review we summarize the advances made in the field of flavoprotein deflavination and reconstitution. Several sophisticated 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. Studies from riboflavinde deficient expression systems and site-directed mutagenesis suggest that the flavinylation reaction is a post-translational, rather than a cotranslational, process. These genetic approaches have also provided insight into the mechanism of covalent flavinylation and the rationale for this atypical protein modi. cation. |
| Databáze: | OpenAIRE |
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