J
Jan A. Berden
Researcher at University of Amsterdam
Publications - 127
Citations - 5895
Jan A. Berden is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Coenzyme Q – cytochrome c reductase & Cytochrome c. The author has an hindex of 36, co-authored 127 publications receiving 5757 citations.
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A functional genomics strategy that uses metabolome data to reveal the phenotype of silent mutations
Léonie M. Raamsdonk,Bas Teusink,David Broadhurst,Nianshu Zhang,Andrew Hayes,Michael C. Walsh,Jan A. Berden,Kevin M. Brindle,Douglas B. Kell,Jem J. Rowland,Hans V. Westerhoff,Karel van Dam,Stephen G. Oliver +12 more
TL;DR: It is demonstrated how the intracellular concentrations of metabolites can reveal phenotypes for proteins active in metabolic regulation, and this approach to functional analysis, using comparative metabolomics, is called FANCY—an abbreviation for functional analysis by co-responses in yeast.
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Prohibitins act as a membrane‐bound chaperone for the stabilization of mitochondrial proteins
Leo G.J. Nijtmans,Liesbeth de Jong,Marta Artal Sanz,Philip J. Coates,Jan A. Berden,Jaap Willem Back,Anton O. Muijsers,Hans van der Spek,Les A. Grivell +8 more
TL;DR: The fact that Phb1/2 is a large multimeric complex, which provides protection of native peptides against proteolysis, suggests a functional homology with protein chaperones with respect to their ability to hold and prevent misfolding of newly synthesized proteins.
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Differential investigation of the capacity of succinate oxidation in human skeletal muscle.
J. C. Fischer,Wim Ruitenbeek,Jan A. Berden,J. M. Frans Trijbels,Jacques H. Veerkamp,Ad M. Stadhouders,Rob C.A. Sengers,Antoon J.M. Janssen +7 more
TL;DR: The results lead to propose the existence of a single acceptor site for phenazine methosulfate at the succinate dehydrogenase complex, not involved in the physiological electron flux across ubiquinone.
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Oxidoreduction of cytochrome b in the presence of antimycin.
Mårten Wikström,Jan A. Berden +1 more
TL;DR: The increased reducibility of cy tochrome b induced by antimycin plus oxidant is considered to be the result of two effects: inhibition of oxidation of ferrocytochrome b by ferricytochrome c1 (the effect of antimyzin), and oxidation of the semiquinone form of a two-equivalent redox couple such as ubiquinone/ubiquinol by the added oxidant, leading to a decreased redox potential of the QH
Journal ArticleDOI
The reaction of antimycin with a cytochrome b preparation active in reconstitution of the respiratory chain
Jan A. Berden,E.C. Slater +1 more
TL;DR: Based on the assumption that the bc1 segment of the respiratory chain contains 2b:1c1:1 antimycin-binding sites, the specific quenching of antimYcin fluorescence by binding to cytochrome b enables an accurate determination of the absorbance coefficients of cytochromes b and c1.