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

@article{Iwata1995StructureA2,
  title={Structure at 2.8 {\AA} resolution of cytochrome c oxidase from Paracoccus denitrificans},
  author={So Iwata and Christian Ostermeier and Bernd Ludwig and Hartmut Michel},
  journal={Nature},
  year={1995},
  volume={376},
  pages={660-669}
}
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. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a3-copper B binuclear centre where molecular oxygen is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be… Expand
Structure at 2.8 Angstrom resolution of cytochrome c oxidase from Paracoccus denitrificans
The crystal structure at 2.8 Angstrom resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment,Expand
Structure and Possible Mechanism of Action of Cytochrome c Oxidase from the Soil Bacterium Paracoccus denitrificans
The four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans were crystallized with the help of antibody Fv fragments. The structure, determined at 2.8-AExpand
Cytochrome c oxidase.
TLDR
The structures form a basis for understanding the mechanism of this redox-coupled transmembrane proton pump, which is the key component of the respiratory chain of most aerobic organisms. Expand
Cytochrome c Oxidase (Heme aa3) from Paracoccus denitrificans: Analysis of Mutations in Putative Proton Channels of Subunit I
TLDR
The properties of the mutated oxidases were analyzed by different methods to elucidate whether they are involved in the coupled and coordinated transfer of protons via two different pathways either to the site of oxygen reduction or through the enzyme from the cytoplasm to the periplasmic side. Expand
High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways.
The structure of the two-subunit cytochrome c oxidase from Paracoccus denitrificans has been refined using X-ray cryodata to 2.25 A resolution in order to gain further insights into its mechanism ofExpand
The Cytochrome c Oxidase from Paracoccus denitrificans Does Not Change the Metal Center Ligation upon Reduction*
TLDR
No ligand exchanges or other major structural changes upon reduction of the cytochrome coxidase from Paracoccus denitrificans were observed, and the three histidine CuB ligands are well defined in the oxidized and in the reduced states. Expand
Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment.
TLDR
The aa3 type cytochrome c oxidase consisting of the core subunits I and II only was isolated from the soil bacterium Paracoccus denitrificans and crystallized as complex with a monoclonal antibody Fv fragment, resulting in well reproducible crystals suitable for high resolution x-ray crystallographic studies. Expand
Primary structure of a novel subunit in ba3‐cytochrome oxidase from thermus thermophilus
TLDR
The ba3‐type cytochrome c oxidase from Thermus thermophilus is known as a two subunit enzyme, and the presence of an additional transmembrane helix “subunit IIa” spanning the membrane is discovered. Expand
Crystal structure of the dihaem cytochrome c4 from Pseudomonas stutzeri determined at 2.2A resolution.
TLDR
The structure of the dihaem cytochrome c4, in conjunction with sequence alignment, suggests that the cytochromes c4 protein has evolved by duplication of a cy tochrome c gene. Expand
Structure at 1.3 A resolution of Rhodothermus marinus caa(3) cytochrome c domain.
TLDR
This is the first high-resolution crystal structure reported for a cytochrome c domain of a caa(3)-type terminal oxidase, and the calculation of the electrostatic potential at the molecular surface of this extra C-terminal domain provides insights into the binding to its redox partner on one side and its interaction with the remaining subunit II on the other side. Expand
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