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The cytochrome c peroxidase and cytochrome c encounter complex: The other side of the story
Author(s) -
Schilder Jesika,
Löhr Frank,
Schwalbe Harald,
Ubbink Marcellus
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.03.055
Subject(s) - cytochrome c peroxidase , cytochrome c , complement (music) , coenzyme q – cytochrome c reductase , chemistry , cytochrome , peroxidase , relaxation (psychology) , paramagnetism , spin (aerodynamics) , chemical physics , computer science , physics , crystallography , biochemistry , biology , enzyme , quantum mechanics , thermodynamics , neuroscience , complementation , mitochondrion , gene , phenotype
Formation of an encounter complex is important for efficient protein complex formation. The encounter state consists of an ensemble of orientations of two proteins in the complex. Experimental description of such ensembles inherently suffers from insufficient data availability. We have measured paramagnetic relaxation enhancements (PRE) on cytochrome c peroxidase (CcP) caused by its partner cytochrome c (Cc) carrying a spin label. The data complement earlier PRE data of spin labelled CcP, identifying several new interactions. This work demonstrates the need of obtaining as many independent data sets as possible to achieve the most accurate description of an encounter complex.