The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å

@article{Tsukihara1996TheWS,
  title={The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 {\AA}},
  author={Tomitake Tsukihara and Hiroshi Aoyama and Eiki Yamashita and Takashi Tomizaki and Hiroshi Yamaguchi and Kyoko Shinzawa-Itoh and Ryosuke Nakashima and Rieko Yaono and Shinya Yoshikawa},
  journal={Science},
  year={1996},
  volume={272},
  pages={1136 - 1144}
}
The crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three phosphatidyl glycerols and two cholates, two hemes A, and three copper, one magnesium, and one zinc. Of 3606 amino acid residues in the dimer, 3560 have been converged to a reasonable structure by refinement. A hydrogen-bonded system, including a propionate of a heme A (heme a), part of peptide… 

Crystal Structure of Bovine Heart Cytochrome c Oxidase at 2.8 Å Resolution

The coordination geometry of CuB and the location of Tyr244 in subunit I at the end of the scalar proton path suggests a hydroperoxo species as the two electron reduced intermediate in the O2 reduction process.

X-ray structure and reaction mechanism of bovine heart cytochrome c oxidase.

The coordination geometry of CuB together with the proximity between the two hemes suggest that heme a, not CuB, donates electrons to initiate the reduction of O2 in the two electron process.

Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia coli at 6 Å resolution

The comparison with the three‐dimensional structure of cytochrome c oxidase shows the clear structural similarity within the common functional core surrounding the metal‐binding sites in subunit I and indicates subtle differences which are due to the distinct subunit composition.

Structure analysis of bovine heart cytochrome c oxidase at 2.8 A resolution.

The crystal structure of bovine heart cytochrome c oxidase has been determined by the multiple isomorphous replacement (MIR) method with three heavy-atom derivatives and the hierarchy of the structural organization of the enzyme complex has been proposed on the basis of intersubunit interactions.

X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution.

Two azide ions were identified, one between the Fe and Cu atoms in the O(2)-reduction site and the other at the transmembrane surface of the enzyme, in the crystal structure of the azide-bound form

Monomeric structure of an active form of bovine cytochrome c oxidase

It is proposed that CcO in the monomeric state, dimeric state, and supercomplex state depending on cardiolipins are involved in regulation of respiratory electron transport, whereas the dimer can be regarded as a physiological standby form in the mitochondrial membrane.

Crystal structure of heme A synthase from Bacillus subtilis

This work determined the crystal structure of HAS from Bacillus subtilis in the apo form at high resolution and reports valuable suggestions of the substrate-heme binding mechanism, which present significant insight into the heme A biosynthesis.

Helix switching of a key active-site residue in the cytochrome cbb3 oxidases.

It is suggested that all of the heme-copper oxidases utilize the same catalytic mechanism and provide an unusual example in which a critical active-site residue originates from different places within the primary sequence for different members of the same superfamily.
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