Structural highlights
Function
[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Publication Abstract from PubMed
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 active than the dominant one. Unlike the high-affinity interaction-extensively studied by X-ray crystallography and NMR spectroscopy-until now the binding of cytochrome c to the low-affinity site has not been observed directly, but inferred mainly from kinetics experiments. Here we report the structure of this elusive, weak protein complex and show that it consists of a dominant, inactive bound species and an ensemble of minor, ET-competent protein-protein orientations, which summarily account for the experimentally determined value of the ET rate constant.
The low-affinity complex of cytochrome c and its peroxidase.,Van de Water K, Sterckx YG, Volkov AN Nat Commun. 2015 May 6;6:7073. doi: 10.1038/ncomms8073. PMID:25944250[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Van de Water K, Sterckx YG, Volkov AN. The low-affinity complex of cytochrome c and its peroxidase. Nat Commun. 2015 May 6;6:7073. doi: 10.1038/ncomms8073. PMID:25944250 doi:http://dx.doi.org/10.1038/ncomms8073
