Title | Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction. |
Publication Type | Journal Article |
Year of Publication | 2013 |
Authors | Volkov, A., and N. A. J. van Nuland |
Journal | J Biomol NMR |
Volume | 56 |
Issue | 3 |
Pagination | 255-63 |
Date Published | 2013 Jul |
ISSN | 1573-5001 |
Keywords | Algorithms, Cytochrome-c Peroxidase, Cytochromes c, Kinetics, Models, Molecular, Molecular Conformation, Nuclear Magnetic Resonance, Biomolecular, Protein Binding |
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. |
DOI | 10.1007/s10858-013-9744-8 |
Alternate Journal | J. Biomol. NMR |
PubMed ID | 23708935 |
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