Publications
Expression, Purification, Characterization, and Solution NMR Study of Highly‐Deuterated Recombinant Yeast Cytochrome c Peroxidase with Enhanced Solubility Vrije Universiteit Brussel
Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase Vrije Universiteit Brussel
Cofactor-dependent structural and binding properties of yeast cytochrome C peroxidase Vrije Universiteit Brussel University of Antwerp
Yeast cytochrome c peroxidase (CcP) is a heme enzyme that reduces hydroperoxides using the electrons provided by its physiological partner cytochrome c (Cc). Contributing to the resistance against the oxidative stress associated with the aerobic metabolism, the Cc-CcP complex has been widely studied and became a paradigm for biological electron transfer. The heme-free, enzymatically inactive apo CcP is the natural precursor of the mature, ...
Expression, purification, characterization, and solution nuclear magnetic resonance study of highly deuterated yeast cytochrome c peroxidase with enhanced solubility Vrije Universiteit Brussel
The low-affinity complex of cytochrome c and its peroxidase Vrije Universiteit Brussel University of Antwerp
The complex of yeast cytochrome c peroxidase and cytochrome c is a paradigm of the biological electron transfer (ET). Building on seven decades of research, two different models have been proposed to explain its functional redox activity. One postulates that the intermolecular ET occurs only in the dominant, high-affinity protein-protein orientation, while the other posits formation of an additional, low-affinity complex, which is much more ...