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PubMed1990

Electron transfer to the binuclear center in cytochrome oxidase: catalytic significance and evidence for an additional intermediate.

We have followed, by transient kinetics, the reduction of cytochrome a3 in the presence of carbon monoxide under different experimental conditions. We have observed that the internal electron transfer rate accounts for the turnover number, and both display the same pH and temperature dependence [pKa = 7.4 and activation energy (Ea) = 14.7 +/- 0.1 kcal/mol]. Moreover, comparison of the time course of cytochrome c oxidation and cytochrome a3 reduction indicates that two electrons are transferred internally and with different rates to the oxygen-binding site. A kinetic model based on sequential internal electron transfer pathways, describing quantitatively the experimental data, is presented and discussed.

Animals↗
PubMed2002

Cytochrome oxidase deficiency in Lowe syndrome.

We report on a patient with complex IV deficiency who in later clinical course was diagnosed as a Lowe syndrome. Mitochondrial abnormalities can be present in Lowe syndrome and might lead to misdiagnosis, additionally because clinical features can be overlapping.

Cytochrome-c Oxidase Deficiency↗
PubMed1998

A case of Ohtahara syndrome with cytochrome oxidase deficiency.

Ohtahara syndrome is a rare cause of epileptic seizures during the neonatal period. This is believed to be the first report of this syndrome with a specific metabolic defect. Defects in respiratory chain function may be more common than previously assumed in patients with this epilepsy syndrome.

Cytochrome-c Oxidase Deficiency↗
PubMed1975

Functional intermediates in reaction of cytochrome oxidase with oxygen.

The development of a low temperature kinetic method for the flash photolysis of the compounds of membrane-bound cytochrome a3 with carbon monoxide in the presence of oxygen affords evidence for three categories of functional intermediate compounds of cytochrome a3 and oxygen. The three classes are identified as follows: Compounds of Type A are considered to be "oxy" compounds of the ferrous heme. They have the composition a3-2+. O2. Compounds of Type B are considered to be peroxide compounds (CU-2+A3-3+ O-2= or CU-2+A3-3+ O2H2) or the equivalent heme Fe-Cu peroxide bridge structures. Compounds of Type C are formed from the ferricyanide pretreated oxidase and may involve higher oxidation states of the heme iron such as quadrivalent iron, and peroxide. Kinetic and equilibrium studies show these compounds to be functional in oxygen reduction in the sequence A yields B yield cytochromes a, c, c1, etc.

Animals↗
PubMed1995

High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes.

When grown in aerated shaking culture, Bacillus subtilis expresses two different haem A-containing terminal oxidases: cytochrome aa3-quinol oxidase and cytochrome caa3 oxidase. This paper describes a high-yield conventional procedure for purifying the two haem A-containing oxidases from the same aerobic culture of Bacillus subtilis. Yields of close to 40% of the total haem A are achieved and about 6 mg of each of the purified oxidases is obtained from 4 litres of liquid culture. Both of the purified enzymes have two subunits, with apparent molecular masses of 71.6 kDa and 34.3 kDa for the cytochrome caa3 oxidase, and 67.6 kDa and 37.2 kDa for aa3-quinol oxidase. These features are in agreement with the sequence data for the corresponding structural genes in the aa3 and caa3 operons of B. subtilis. Some spectral and enzymic features of the two purified oxidases are reported that are consistent with the inclusion of both of these enzymes as members of the cytochrome oxidase superfamily.

Bacillus subtilis↗
PubMed1983

An mRNA maturase is encoded by the first intron of the mitochondrial gene for the subunit I of cytochrome oxidase in S. cerevisiae.

We have localized ten oxi3- mutations in the first, al1, intron of the coxl gene. All are splicing deficient, being unable to excise the intron. Complementation experiments disclose several domains in the intron al1: the 5'-proximal and 3'-proximal domains harbor cis-dominant mutations, while trans-recessive ones are located in the intron's open reading frame. Comprehensive analyses of allele-specific polypeptides accumulating in mutants show that they result from the translation of the intron's ORF. We conclude that a specific mRNA maturase involved in splicing of oxidase mRNA is encoded by the intron al1 in a manner similar to the cytochrome b mRNA maturase.

Chromosome Mapping↗