1U75

Electron Transfer Complex between Horse Heart Cytochrome c and Zinc-Porphyrin Substituted Cytochrome c Peroxidase

Summary for 1U75

• Entry DOI: 10.2210/pdb1u75/pdb
• Related: 1U74
• Descriptor: cytochrome c peroxidase, Cytochrome c, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: protein-protein complex, heme, oxidoreductase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Mitochondrion matrix: P00004
• Total number of polymer chains: 3
• Total formula weight: 81325.35

Authors

Crane, B.R.,Kang, S.A. (deposition date: 2004-08-02, release date: 2004-09-28, Last modification date: 2024-12-25)

Primary citation

Kang, S.A.,Marjavaara, P.J.,Crane, B.R.
Electron transfer between cytochrome c and cytochome c peroxidase in single crystals.
J.Am.Chem.Soc., 126:10836-10837, 2004

PubMed Abstract: 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.

PubMed: 15339156
DOI: 10.1021/ja049230u

Experimental method

X-RAY DIFFRACTION (2.55 Å)