3aso | pdb_00003aso

Bovine heart cytochrome C oxidase in the fully oxidized state measured at 0.9 angstrom wavelength

spinqualitylabelsall models 3aso, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3aso is a 20 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CDL, CHD, CU, CUA, DMU, FME, HEA, MG, NA, PEK, PGV, PSC, SAC, TGL, TPO, UNX, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COX5A_BOVIN This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Publication Abstract from PubMed Fully oxidized cytochrome c oxidase (CcO) under enzymatic turnover is capable of pumping protons, while fully oxidized CcO as isolated is not able to do so upon one-electron reduction. The functional difference is expected to be a consequence of structural differences: [Fe(3+)-OH(-)] under enzymatic turnover versus [Fe(3+)-O(2)(2-)-Cu(2+)] for the as-isolated CcO. However, the electron density for O(2)(2-) is equally assignable to Cl(-). An anomalous dispersion analysis was performed in order to conclusively demonstrate the absence of Cl(-) between the Fe(3+) and Cu(2+). Thus, the peroxide moiety receives electron equivalents from cytochrome c without affecting the oxidation states of the metal sites. The metal-site reduction is coupled to the proton pump. Distinguishing between Cl- and O2(2-) as the bridging element between Fe3+ and Cu2+ in resting-oxidized cytochrome c oxidase.,Suga M, Yano N, Muramoto K, Shinzawa-Itoh K, Maeda T, Yamashita E, Tsukihara T, Yoshikawa S Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):742-4. Epub 2011 Jul 12. PMID:21795816 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c oxidase 3D structures

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