Cytochrome oxidase evolved by tinkering with denitrification enzymes

@article{Saraste1994CytochromeOE,
  title={Cytochrome oxidase evolved by tinkering with denitrification enzymes},
  author={Matti Saraste and Jose Castresana},
  journal={FEBS Letters},
  year={1994},
  volume={341}
}

The bacterial cytochrome cbb3 oxidases.

Structure and evolution of cytochrome oxidase

The structural features of cytochrome oxidases are reviewed in light of their evolution and it is shown that these enzymes, exemplified by the rhizobial FixN complex, probably remind the first oxidases.

Identification of the Genes Encoding Nitric Oxide Reductase in the Aerobic Photosynthetic Bacterium Roseobacter denitrificans OCh114

A cytochrome bc-type complex of Roseobacter denitrificans OCh114 was thought to be a novel cytochrome c oxidase. To determine its function, we deleted the genes encoding the complex. The mutant grew

The bacterial respiratory nitric oxide reductase.

Progress towards understanding the pathways of electron and proton transfer in NOR is considered and how this information can be integrated with evidence for the likely modes of substrate binding at the active site to propose a revised and experimentally testable reaction mechanism.

Enzyme diversity and mosaic gene organization in denitrification

The biochemical investigation of denitrification has culminated in the description of the crystal structures of the two types of nitrite reductases, ancestor of energy-conserving enzymes of the heme-copper oxidase superfamily.

The role of the nirQOP genes in energy conservation during anaerobic growth of Pseudomonas aeruginosa.

Phylogenetic analysis showed that NirO belongs to the family of subunit III of cytochrome oxidases but is distantly related to the other bacterial or mitochondrial proteins.
...

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  • M. Saraste
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    Quarterly reviews of biophysics
  • 1990
This article tries to be a compact summary of some recent research on cytochrome c oxidase (EC 1.9.3.1), an important enzyme in membrane bioenergetics, because the protein-bound haems are functionally and spectroscopically different.

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