1ocr: Difference between revisions

Revision as of 17:21, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ocr.png

Template:STRUCTURE 1ocr

BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATEBOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE

Template:ABSTRACT PUBMED 9624044

About this StructureAbout this Structure

1OCR is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase., Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T, Science. 1998 Jun 12;280(5370):1723-9. PMID:9624044

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE'''
+===BOVINE HEART CYTOCHROME C OXIDASE IN THE FULLY REDUCED STATE===
-==Overview==
+<!--
-Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_9624044}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9624044}}
 ==About this Structure==
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 [[Category: Cytochrome c oxidase]]
 [[Category: Reduced]]
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