1u75
Electron Transfer Complex between Horse Heart Cytochrome c and Zinc-Porphyrin Substituted Cytochrome c Peroxidase
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OverviewOverview
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.
About this StructureAbout this Structure
1U75 is a Protein complex structure of sequences from Equus caballus and Saccharomyces cerevisiae with , and as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Full crystallographic information is available from OCA.
ReferenceReference
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
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