1u75: Difference between revisions

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{{STRUCTURE_1u75|  PDB=1u75  |  SCENE=  }}  
{{STRUCTURE_1u75|  PDB=1u75  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_15339156}}


==About this Structure==
==About this Structure==
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[[Category: Heme]]
[[Category: Heme]]
[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
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Revision as of 23:33, 27 July 2008

File:1u75.png

Template:STRUCTURE 1u75

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

Template:ABSTRACT PUBMED 15339156

About this StructureAbout this Structure

1U75 is a Protein complex structure of sequences from Equus caballus and Saccharomyces cerevisiae. 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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