PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “CYTOCHROME OXIDASE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 127 records · Page 7Linked to original sources
PubMed2004

Differences in two Pseudomonas aeruginosa cbb3 cytochrome oxidases.

Bacterial cytochrome cbb3 oxidases are members of the haeme-copper oxidase superfamily that are important for energy conservation by a variety of proteobacteria under oxygen-limiting conditions. The opportunistic pathogen Pseudomonas aeruginosa is unusual in possessing two operons that each potentially encode a cbb3 oxidase (cbb3-1 or cbb3-2). Our results demonstrate that, unlike typical enzymes of this class, the cbb3-1 oxidase has an important metabolic function at high oxygen tensions. In highly aerated cultures, cbb3-1 abundance and expression were greater than that of cbb3-2, and only loss of cbb3-1 influenced growth. Also, the activity of cbb3-1, not cbb3-2, inhibited expression of the alternative oxidase CioAB and thus influenced a signal transduction pathway much like that found in the alpha-proteobacterium Rhodobacter sphaeroides. Cbb3-2 appeared to play a more significant role under oxygen limitation by nature of its increased abundance and expression compared to highly aerated cultures, and the regulation of the cbb3-2 operon by the putative iron-sulphur protein Anr. These results indicate that each of the two P. aeruginosa cbb3 isoforms have assumed specialized energetic and regulatory roles.

Aerobiosis↗
PubMed1983

Lipid requirements for coupled cytochrome oxidase vesicles.

Cytochrome c oxidase has been reconstituted with two synthetic phospholipids, dioleoylphosphatidylcholine and dioleoylphosphatidylethanolamine. Vesicles prepared from either of these two lipids alone showed no stimulation of enzyme activity upon addition of carbonyl cyanide (trifluoromethoxy)phenylhydrazone and valinomycin, indicating that they were leaky to small ions. However, when mixtures of the two lipids were used for the reconstitution, tightly coupled vesicles could be obtained. The coupling ratio was dependent upon the ratio of dioleoylphosphatidylcholine to dioleoylphosphatidylethanolamine and also on the lipid-to-protein ratio. Maximal rates of enzyme activity were not significantly different with different lipid mixtures. The results are discussed in terms of both the size distribution of the reconstituted vesicles and the possible requirement for a variety of lipid species to ensure tight sealing at the lipid-protein interface.

Animals↗
PubMed1994

Decrease in cytochrome c oxidase and cytochrome oxidase subunit I messenger RNA levels in preeclamptic pregnancies.

OBJECTIVE: To elucidate the possible relation between mitochondrial gene expression and placental dysfunction. METHODS: We measured the activity of cytochrome c oxidase and the expression of cytochrome oxidase subunit I in mitochondria from human placentas of women whose gestations were appropriate for gestational age (AGA) and those with preeclampsia. In addition, the amounts of normal mtDNA and deleted mitochondrial DNA were examined in the two groups by Southern blot analysis and polymerase chain reaction, respectively. RESULTS: Cytochrome c oxidase activity and expression of cytochrome oxidase subunit I were significantly lower in the preeclamptic group than in the AGA group. There were no differences between the groups in the amounts of mitochondrial DNA. In addition, no mutant mitochondrial DNA with a 4977-base pair deletion was detected in the two groups. CONCLUSION: These results suggest that reduced expression of the mitochondrial gene is involved in placental dysfunction in preeclamptic pregnancy.

Actins↗
PubMed2000

A human SCO2 mutation helps define the role of Sco1p in the cytochrome oxidase assembly pathway.

Deficiencies in cytochrome oxidase, the terminal enzyme of the mitochondrial respiratory chain, are most often caused by an inability to complete assembly of the enzyme. Pathogenic mutations in SCO2, which encodes a cytochrome oxidase assembly factor, were recently described in several cases of fatal infantile cardioencephalomyopathy. To determine the molecular etiology of these disorders, we describe the generation and characterization of the parallel mutations in the homologous yeast SCO1 gene. We show that the E155K yeast sco1 mutant is respiration-competent, whereas the S240F mutant is not. Interestingly, the S240F mutation allows partial but incorrect assembly of cytochrome oxidase, as judged by an altered cytochrome aa(3) peak. Immunoblot analysis reveals a specific absence of subunit 2 from the cytochrome oxidase in this mutant. Taken together, our data suggest that Sco1p provides copper to the Cu(A) site on subunit 2 at a step occurring late in the assembly pathway. This is the first instance of a yeast cytochrome oxidase assembly mutant that is partially assembled. The S240F mutant also represents a powerful new tool with which to elucidate further steps in the cytochrome oxidase assembly pathway.

Carrier Proteins↗
PubMed2000

Human cytochrome oxidase deficiency.

The human cytochrome oxidase complex is a multisubunit assembly in the inner mitochondrial membrane responsible for the terminal event in electron transport in which molecular oxygen is reduced. Various phenotypic forms of cytochrome oxidase deficiency have been recognized, the major varieties involving degeneration of the brain stem and basal ganglia (Leigh syndrome) and lactic acidemia. Others include a fatal infantile form, a benign reversible form, and forms with cardiomyopathy. Early recognition of complementation groups within, for instance, the Leigh syndrome group has recently been followed up with a description of the gene defect for three of the nuclear-encoded forms of cytochrome c oxidase (COX) deficiency. The three genes indicted, SURF1 for Leigh syndrome, COX 10 for leukodystrophy and tubulopathy, and SCO2 for the cardiomyopathic form, all have a role in the assembly of the mature cytochrome oxidase complex. The description of these gene defects and the role these genes play are discussed in terms of what can be learned about COX assembly and about the etiology of the different phenotypic forms of the disease.

Alkyl and Aryl Transferases↗
PubMed1980

Cytochrome oxidase: an alternative model.

Oxidative titration of reduced cytochrome oxidase (cytochrome c oxidase; ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) in the presence of carbon monoxide and sulfide, at potentials greater than +500 mV (vs. the neutral hydrogen electrode), have failed to produce new copper signals in the electron paramagnetic resonance spectrum of this enzyme. This observation implies that once of the copper centers in cytochrome oxidase remains Cu(I) under strongly oxidizing conditions. The rationalization of this fact, and the possible explanation of a great accumulation of spectroscopic data, is that cytochrome a3 may be a two-electron redox center, with stable Fe(IV), Fe(III), and Fe(II) states during its redox cycle. This oxidase model does not require an antiferromagnetic coupling scheme, in contrast to currently prevalent models.

Animals↗
PubMed2005

Analysis of COX2 mutants reveals cytochrome oxidase subassemblies in yeast.

Cytochrome oxidase catalyses the reduction of oxygen to water. The mitochondrial enzyme contains up to 13 subunits, 11 in yeast, of which three, Cox1p, Cox2p and Cox3p, are mitochondrially encoded. The assembly pathway of this complex is still poorly understood. Its study in yeast has been so far impeded by the rapid turnover of unassembled subunits of the enzyme. In the present study, immunoblot analysis of blue native gels of yeast wild-type and Cox2p mutants revealed five cytochrome oxidase complexes or subcomplexes: a, b, c, d and f; a is likely to be the fully assembled enzyme; b lacks Cox6ap; d contains Cox7p and/or Cox7ap; f represents unassembled Cox1p; and c, observed only in the Cox2p mutants, contains Cox1p, Cox3p, Cox5p and Cox6p and lacks the other subunits. The identification of these novel cytochrome oxidase subcomplexes should encourage the reexamination of other yeast mutants.

Electron Transport Complex IV↗
PubMedDate not supplied

The effects of cyanide on brain mitochondrial cytochrome oxidase and respiratory activities.

Brain mitochondrial cytochrome oxidase and respiratory activities were compared after in vivo and in vitro exposure to cyanide. For the in vivo studies, mice were exposed to a non-lethal (4 mg kg-1) or lethal (20 mg kg-1) dose of KCN. From these mice, purified brain mitochondria were prepared and cytochrome oxidase and respiratory activities measured. Results of these experiments revealed greater inhibition of cytochrome oxidase activity following a lethal (20 mg kg-1) than a non-lethal (4 mg kg-1) KCN dose (57 and 45% inhibition, respectively). Respiration states 3 and 4 of brain mitochondria prepared from mice that received 4 mg kg-1 KCN were inhibited by 15 and 20%, respectively. In mice that received a lethal 20 mg kg-1 KCN dose, respiration states 3 and 4 were each inhibited by ca. 30% (P < 0.05). In vitro, mitochondrial cytochrome oxidase activity was inhibited in a concentration-dependent fashion at cyanide concentrations of 10(-6)-10(-2) M. A biphasic inhibition of ADP-stimulated (state 3) respiration was observed. Cyanide concentrations of 10(-6)-10(-4) M produced only a 25% inhibition of respiration state 3, whereas 10(-3) M produced 80% inhibition. Because this dramatic inhibition only occurred at cyanide concentrations that caused > 50% inhibition of mitochondrial cytochrome oxidase activity, these findings suggest that a large proportion of cytochrome oxidase activity may be functional reserve and that cyanide poisoning likely involves other mechanisms in addition to inhibition of cytochrome oxidase.

Adenosine Diphosphate↗
PubMed1987

Identification and properties of a quinol oxidase super-complex composed of a bc1 complex and cytochrome oxidase in the thermophilic bacterium PS3.

Evidence for the presence of a quinol oxidase super-complex composed of a cytochrome bc1 complex and cytochrome oxidase in the respiratory chain of a Gram-positive thermophilic bacterium PS3 is reported. On incubation with an octyl glucoside-solubilized fraction of the total membranes of PS3 anti-serum against PS3 cytochrome oxidase gave an immunoprecipitate that showed both quinol-cytochrome c reductase and cytochrome c oxidase activities. When the cholate-deoxycholate and LiCl-treated membranes of PS3 were solubilized and subjected to ion-exchange chromatography in the presence of octaethyleneglycol dodecyl ether, most of the A-, B-, and C-type cytochromes were copurified as a peak having both quinol-cytochrome c reductase and cytochrome oxidase activities. The immunoprecipitate and quinol oxidase preparation contained hemes a, b, and c in a ratio of about 2:2:3, indicating the presence of one-to-one complex of cytochrome oxidase containing 2 hemes a and one heme c, and a bc1 complex containing 2 hemes b and 2 hemes c. Gel electrophoresis in the presence of dodecyl sulfate showed that the immunoprecipitate and quinol oxidase preparation were composed of seven subunits; those of 51 (56-kDa), 38, and 22 kDa for cytochrome oxidase and those of 29, 23, 21, and 14 kDa for the bc1 complex. The 38-, 29-, and 21 kDa components possessed covalently bound heme c. The apparent molecular mass of the super complex was estimated to be as 380 kDa by gel filtration.

Antibodies↗