Structural highlights
Function
CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cytochrome c (Cc) and cytochrome c peroxidase (CcP) form an important redox pair for understanding interprotein electron transfer (ET). Measurements of ET rates from photoexcited CcP substituted with Zn porphyrin to either yeast Fe(III)Cc or horse Fe(III)Cc in crystals reveal that the molecular associations found in the respective crystal structures determine solution reactivity. Similar forward rates for yeast isozyme-1 Cc (yCc) and yCc homologue horse Cc (hCc), despite different orientations relative to CcP, suggest small-amplitude conformational gating of ET even in the crystalline state; faster back ET in the yCc compared to the hCc complex agrees with the relative coupling between redox sites predicted by the structures.
Electron transfer between cytochrome c and cytochome c peroxidase in single crystals.,Kang SA, Marjavaara PJ, Crane BR J Am Chem Soc. 2004 Sep 8;126(35):10836-7. PMID:15339156[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kang SA, Marjavaara PJ, Crane BR. Electron transfer between cytochrome c and cytochome c peroxidase in single crystals. J Am Chem Soc. 2004 Sep 8;126(35):10836-7. PMID:15339156 doi:http://dx.doi.org/10.1021/ja049230u
