Cytochrome oxidase evolved by tinkering with denitrification enzymes

  title={Cytochrome oxidase evolved by tinkering with denitrification enzymes},
  author={Matti Saraste and Jose Castresana},
  journal={FEBS Letters},

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.



An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes.

The homology between the sox gene products and their mitochondrial counterparts suggests that energy conservation coupled to the quinol oxidation catalysed either by the Sulfolobus oxidase or two mitochondrial respiratory enzymes may have a similar mechanism.

The happy family of cytochrome oxidases.

This short review will focus on bacterial quinol and cytochrome c oxidases, both of which are known to have subunits homologous to those in the mitochondrial enzyme but which contain different prosthetic groups.

Cytochrome aa3 from Sulfolobus acidocaldarius. A single-subunit, quinol-oxidizing archaebacterial terminal oxidase.

A novel type of cytochrome aa3 is postulated in this paper which oxidizes reduced quinones as an artificial single-electron donor as well as reduced caldariella quinone, which is assumed to represent the natural substrate.

Pseudomonas stutzeri N2O reductase contains CuA-type sites.

N2O reductase (N2O----N2) is the terminal enzyme in the energy-conserving denitrification pathway of soil and marine denitrifying bacteria. The protein is composed of two identical subunits and

The nitric oxide reductase of Paracoccus denitrificans.

The nitric oxide (NO) reductase activity of the cytoplasmic membrane of Paracoccus denitrificans can be solubilized in dodecyl maltoside with good retention of activity, supporting the view that NO reduct enzyme is a discrete enzyme that participates in the denitrification process.

Structural features of cytochrome oxidase.

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

EPR studies of cytochrome aa3 from Sulfolobus acidocaldarius. Evidence for a binuclear center in archaebacterial terminal oxidase.

The purified cytochrome aa3-type oxidase from Sulfolobus acidocaldarius (DSM 639) consists of a single subunit, containing one low-spin and one high-spin A-type hemes and copper, indicating that this enzyme contains only a CUB-type center.