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Gewählte Publikation:

Kadek, A; Kavan, D; Felice, AK; Ludwig, R; Halada, P; Man, P; .
(2015): Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase.
FEBS Lett. 2015; 589(11):1194-1199 FullText FullText_BOKU

Abstract:
Cellobiose dehydrogenase (CDH) from wood degrading fungi represents a subclass of oxidoreductases with unique properties. Consisting of two domains exhibiting interdomain electron transfer, this is the only known flavocytochrome involved in wood degradation. High resolution structures of the separated domains were solved, but the overall architecture of the intact protein and the exact interface of the two domains is unknown. Recently, it was shown that divalent cations modulate the activity of CDH and its pH optimum and a possible mechanism involving bridging of negative charges by calcium ions was proposed. Here we provide a structural explanation of this phenomenon confirming the interaction between negatively charged surface patches and calcium ions at the domain interface. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Autor/innen der BOKU Wien:
Felice Alfons Konrad
Ludwig Roland
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Calcium/chemistry*;Carbohydrate Dehydrogenases/chemistry*;Electron Transport/physiology;Fungal Proteins/chemistry*;Protein Structure, Tertiary;Sordariales/enzymology*;Structure-Activity Relationship;

Find related publications in this database (Keywords)
Hydrogen/deuterium exchange
Cellobiose dehydrogenase
Calcium effect
Interdomain electron transfer
Flavocytochrome
Electrostatic interaction


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