[NMR paper] Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.

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Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.

Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.

J Biomol NMR. 2013 May 25;

Authors: Volkov AN, van Nuland NA

Abstract
Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution. Combining the Cc- and CcP-detected experiments, the binding interface on both proteins was mapped out, confirming that the X-ray structure of the complex is maintained in solution. Using NMR titrations and chemical shift perturbation analysis, we show that the interaction is independent of the CcP spin-state and is only weakly affected by the Cc redox state. Based on these findings, we argue that the complex of the ferrous Cc and the cyanide-bound CcP is a good mimic of the catalytically-active Cc-CcP compound I species. Finally, no chemical shift perturbations due to the Cc binding at the low-affinity CcP site were observed at low ionic strength. We discuss possible reasons for the absence of the effects and outline future research directions.


PMID: 23708935 [PubMed - as supplied by publisher]



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