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Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase

The flavoenzyme DAAO from Rhodotorula gracilis, a structural paradigm of the glutathione-reductase family of flavoproteins, is a stable homodimer with a flavin adenine dinucleotide (FAD) molecule tightly bound to each 40-kD subunit. In this work, the thermal unfolding of dimeric DAAO was compared wi...

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Bibliografiska uppgifter
Huvudupphovsmän: Pollegioni, Loredano, Iametti, Stefania, Fessas, Dimitrios, Caldinelli, Laura, Piubelli, Luciano, Barbiroli, Alberto, Pilone, Mirella S., Bonomi, Francesco
Materialtyp: Artigo
Språk:Inglês
Publicerad: Cold Spring Harbor Laboratory Press 2003
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Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323872/
https://ncbi.nlm.nih.gov/pubmed/12717024
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