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1oco
From Proteopedia
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BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND 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.
About this Structure
1OCO is a [Protein complex] structure of sequences from [Bos taurus] with CU, MG, NA, ZN, HEA and CMO as [ligands]. The following pages contain interesting information on the relation of 1OCO with [Cytochrome c Oxidase]. Active as [[1]], with EC number [1.9.3.1]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 22:09:55 2007
