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

  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},
  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.



Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A

The high resolution three-dimensional x-ray structure of the metal sites of bovine heart cytochrome c oxidase is reported, suggesting a dinuclear copper center with an unexpected structure similar to a [2Fe-2S]-type iron-sulfur center.

Topology of subunits of the mammalian cytochrome c oxidase: relationship to the assembly of the enzyme complex.

The arrangement of three subunits of beef heart cytochrome c oxidase, subunits Va, VIa, and VIII, has been explored by chemical labeling and protease digestion studies and shows a transmembrane orientation.

Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

The crystal structure at 2.8 Å resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is described and mechanisms for proton pumping are discussed.

Possible proton relay pathways in cytochrome c oxidase.

An important role for the conserved II-III loop in the proton pumping process is supported and the activity of the reconstituted Asp132 mutants was inhibited rather than stimulated by ionophores or uncoupler, supporting the possibility of involvement of residues in helix VIII and the IX-X loop.

The histidine cycle: A new model for proton translocation in the respiratory heme-copper oxidases

A model of redox-linked proton translocation of the oxygenous ligand on the iron in the binuclear heme-copper site through an electrostatic nonbonding interaction between this ligand and the doubly protonated imidazolium group of a conserved histidine residue nearby is presented.

Cytochrome c oxidase in Neurospora crassa contains myristic acid covalently linked to subunit 1.

The [3H]myristate, which was chemically recovered from the radiolabeled subunit peptide, modified an invariant Lys-324, based upon analyses of proteolysis products, represents an uncommon type of myristoylation through an amide linkage at an internal lysine, rather than an N-terminal glycine.

Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity.

It is proposed that an acidic residue at position 135 in subunit I of cytochrome bo may be important to form a functional proton input channel of the proton pump.

Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn.

Results suggest that the C-terminal part of the domain may be alpha-helical and that the entire "loop" plays an important structural and functional role as part of an input channel of the proton translocation machinery.