2occ: Difference between revisions

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==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.

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==

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[[Category: oxidoreductase]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 26: / Line 26: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:46:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:52 2008''