The proton pump of heme‐copper oxidases.

  title={The proton pump of heme‐copper oxidases.},
  author={Sergio Papa and Nazzareno Capitanio and Philippe Glaser and Gaetano Villani},
  journal={Cell Biology International},
Proton pumping heme‐copper oxidases represent the terminal, energy‐transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB‐heme a3 (or heme o) binuclear center, associated with the largest subunit I of cytochrome c and quinol oxidases, is directly involved in the coupling between dioxygen reduction and proton pumping. The role of the other subunits is less clear. The following aspects will be covered in this paper:i) the efficiency of coupling in the mitochondrial aa3… 

Mechanism of Proton-Motive Activity of Heme-Copper Oxidases

Recent ideas are reviewed on some of the critical features that likely underlie the mechanism of coupling of proton and electron transfers and to relate them to the available structural information.

Probing a Role of Subunit IV of the Escherichia coli bo-type Ubiquinol Oxidase by Deletion and Cross-linking Analyses*

It is proposed that subunit IV is present in a cleft formed by subunits I and III and assists the CuB binding to subunit I during biosynthesis or assembly of the oxidase complex.

Proton Pumps of Respiratory Chain Enzymes

Proticity is essentially used to drive phosphorylation of ADP to ATP by the FOF1-ATP synthase of coupling membranes and can drive solute transport by proton coupled transporters and mechanical work as in bacterial flagella, and can result in heat production in brown adipose tissue mitochondria.

The molecular and cellular basis of copper dysregulation and its relationship with human pathologies

An overview of the current knowledge of Cu metabolism and transport and its relation to various human pathologies is provided.

Antagonisme de lactococcus garvieae vis-à-vis de Staphylococcus aureus : étude physiologique et transcriptomique des mécanismes

L’objectif de cette these etait de caracteriser l’antagonisme de L. garvieae N201, isole de fromage, vis-a-vis de souches de S. aureus par des approches in vitro : genomique, transcriptomique (ciblee concernant S.aureus, globale concernant L.Aureus) and phenotypique.

Separation and analysis of Bacillus subtilis respiratory chain complexes

A b6c + caa3 supercomplex of 600 kDa and SQR, aa3, and NADH dehydrogenase is obtained by dodecyl maltoside solubilization and separation of the respiratory chain components by ionic exchange chromatography.



The gateway to the active site of heme-copper oxidases.

The spectroscopy and dynamics of CO binding were measured for wild-type and mutant cytochromes bo, members of the superfamily of heme-copper oxidases. The results suggest that access of ligands,

Possible Protonmotive Osmochemistry in Cytochrome Oxidase a

  • P. Mitchell
  • Chemistry, Biology
    Annals of the New York Academy of Sciences
  • 1988
Following nearly eight years of controversy, after Wikstrirm began in 1977 to cite evidence in favor of a redox-linked proton-pumping function in cytochrome oxidase, it has become widely agreed that cyto chrome oxidase is protonmotive as well as electronmotive.

Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation

  • W. Woodruff
  • Chemistry
    Journal of bioenergetics and biomembranes
  • 1993
Results are presented which suggest a general mechanism for the entry and binding of exogenous ligands at the “binuclear site” (CuB Fea3) of the heme-copper oxidases and it is suggested that these ligand shuttle reactions might be functionally important in providing a coupling mechanism for electron transfer and proton translocation.

Structure and function of cytochrome-c oxidase.

Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa3 and cytochromebo

A summary of site-directed mutants of conserved residues in these two enzymes is presented and discussed in terms of a current model of the structure of the metal centers and evidence for regions of the protein likely to be involved in proton transfer.

Oxygen activation and the conservation of energy in cell respiration

The molecular mechanism of 02 reduction and its linkage to H+ translocation are now emerging and the bimetallic haem iron–copper reaction centre in this family of enzymes is the critical structure for catalysis of both these processes.