8gvm

The structure of azide-bound cytochrome C oxidase determined using the crystals exposed to 20 mm azide solution for 4 days

spinqualitylabelsall models 8gvm, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8gvm 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 1.851Å Ligands: AZI, CDL, CHD, CU, CUA, DMU, EDO, FME, HEA, MG, NA, PEK, PGV, PSC, SAC, TGL, TPO, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COX1_BOVIN Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. Publication Abstract from PubMed Cytochrome c oxidase (CcO) is the terminal oxidase of cellular respiration, reducing O2 to water and pumping protons. X-ray structural features have suggested that CcO pumps protons via a mechanism involving electrostatic repulsions between pumping protons in the hydrogen bond network of a proton-conducting pathway (the H-pathway) and net positive charges created upon oxidation of an iron site, heme alpha (Fe alpha(2+)), for reduction of O2 at another iron site, heme alpha3 (Fe alpha3(2+)). The protons for pumping are transferred to the hydrogen bond network from the N-side via the water channel of the H-pathway. Back-leakage of protons to the N-side is thought to be blocked by closure of the water channel. To experimentally test this, we examined X-ray structures of the azide-bound, oxidized bovine CcO and found that an azide derivative (N3(-)-Fe alpha3(3+), CuB(2+)-N3(-)) induces a translational movement of the heme alpha3 plane. This was accompanied by opening of the water channel, revealing that Fe alpha3 and the H-pathway are tightly coupled. The channel opening in the oxidized state is likely to induce back-leakage of pumping protons which lowers the proton level in the hydrogen bond network during enzymatic turnover. The proton level decrease weakens the electron affinity of Fe alpha , if Fe alpha electrostatically interacts with protons in the hydrogen bond network. The previously reported azide-induced redox-potential decrease in Fe alpha supports existence of the electrostatic interaction. In summary, our results indicate that the H-pathway is critical for CcO's proton-pumping function. X-ray structural analyses of azide-bound cytochrome c oxidases reveal that the H-pathway is critically important for the proton-pumping activity.,Shimada A, Hatano K, Tadehara H, Yano N, Shinzawa-Itoh K, Yamashita E, Muramoto K, Tsukihara T, Yoshikawa S J Biol Chem. 2018 Aug 3. pii: RA118.003123. doi: 10.1074/jbc.RA118.003123. PMID:30077971 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c oxidase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA