Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 327506
Title Deflavination and reconstitution of proteins. Tackling fold and function
Author(s) Hefti, M.H.; Vervoort, J.J.M.; Berkel, W.J.H. van
Source European Journal of Biochemistry 270 (2003). - ISSN 0014-2956 - p. 4227 - 4242.
Department(s) Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2003
Keyword(s) amino-acid oxidase - flavin-adenine-dinucleotide - p-hydroxybenzoate hydroxylase - active-site probes - riboflavin-binding-protein - nuclear-magnetic-resonance - desulfovibrio-vulgaris flavodoxin - megasphaera-elsdenii flavodoxin - butyryl-coa dehydrogenase - apop
Abstract 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.
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