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PubMed2004

COX23, a homologue of COX17, is required for cytochrome oxidase assembly.

Deletion of reading frame YHR116W of the Saccharomyces cerevisiae nuclear genome elicits a respiratory deficiency. The encoded product, here named Cox23p, is shown to be required for the expression of cytochrome oxidase. Cox23p is homologous to Cox17p, a water-soluble copper protein previously implicated in the maturation of the Cu(A) center of cytochrome oxidase. The respiratory defect of a cox23 null mutant is rescued by high concentrations of copper in the medium but only when the mutant harbors COX17 on a high copy plasmid. Overexpression of Cox17p by itself is not a sufficient condition to rescue the mutant phenotype. Cox23p, like Cox17p, is detected in the intermembrane space of mitochondria and in the postmitochondrial supernatant fraction, the latter consisting predominantly of cytosolic proteins. Because Cox23p and Cox17p are not part of a complex, the requirement of both for cytochrome oxidase assembly suggests that they function in a common pathway with Cox17p acting downstream of Cox23p.

Amino Acid Sequence↗

PubMed1980

Characterization of the intermediates in the reaction of membrane-bound mixed-valence-state cytochrome oxidase with oxygen at low temperatures by optical spectroscopy in the visible region.

The 'pure' difference spectra of the three species, IM, IIM and IIIM, formed in the low-temperature reaction of membrane-bound mixed-valence-state cytochrome oxidase with O2 relative to unliganded membrane-bound mixed-valence-state cytochrome oxidase were characterized by optical spectroscopy in the visible region. The difference spectrum of species IM was characterized by a peak at 590 nm and a trough at 608 nm, that of species IIM by a peak at 606 nm, and that of species IIIM by a peak at 610 nm. A comparison with the difference spectra of species IIM and IIIM obtained with soluble cytochrome oxidase [Clore, Andréasson, Karlsson, Aasa & Malmström (1980) Biochem. J. 185, 155-167] revealed small but significant differences in the peak positions and bandwidths of the 605-610 nm absorption band.

Animals↗

PubMed1982

Proton translocation stoichiometry of cytochrome oxidase: use of a fast-responding oxygen electrode.

The mechanistic stoichiometry of vectorial H+ ejection coupled to electron transport from added ferrocytochrome c to oxygen by the cytochrome oxidase (EC 1.9.3.1) of rat liver mitoplasts was determined from measurements of the initial rates of electron flow and H+ ejection in the presence of K+ (with valinomycin). Three different methods of measuring electron flow were used: (a) dual-wavelength spectrophotometry of ferrocytochrome c oxidation, (b) uptake of scalar H+ for the reduction of O2 in the presence of a protonophore, and (c) a fast-responding membraneless oxygen electrode. The reliability of the rate measurements was first established against the known stoichiometry of the scalar reaction of cytochrome oxidase (2ferrocytochrome c + 2H+ + 1/2O2 leads to 2ferricytochrome c + H2O) in the presence of excess protonophore. With all three methods the directly observed vectorial H+/O ejection ratios in the presence of K+ + valinomycin significantly exceeded 3.0. However, because the rate of backflow of the ejected H+ into the mitoplasts is very high and increases with the increasing delta pH generated across the membrane, there is a very rapid decline in the observed H+/O ratio from the beginning of the reaction. Kinetic analysis of ferrocytochrome c oxidation by the mitoplasts, carried out with a fast-responding membraneless oxygen electrode, showed the reaction to be first order in O2 and allowed accurate extrapolation of the rates of O2 uptake and H+ ejection to zero time. At this point, at which there is zero delta pH across the membrane, the H+/O ejection ratio of the cytochrome oxidase reaction, obtained from the rates at zero time, is close to 4.0.

Chemical Phenomena↗

PubMed1996

Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule.

We have studied the kinetics of the oxygen reaction of the fully reduced quinol oxidase, cytochrome bo3, using flow-flash and stopped flow techniques. This enzyme belongs to the heme-copper oxidase family but lacks the CuA center of the cytochrome c oxidases. Depending on the isolation procedure, the kinetics are found to be either nearly monophasic and very different from those of cytochrome c oxidase or multiphasic and quite similar to cytochrome c oxidase. The multiphasic kinetics in cytochrome c oxidase can largely be attributed to the presence Of CuA as the donor of a fourth electron, which rereduces the originally oxidized low-spin heme and completes the reduction of O2 to water. Monophasic kinetics would thus be expected, a priori, for cytochrome bo3 since it lacks the CuA center, and in this case we show that the oxygen reaction is incomplete and ends with the ferryl intermediate. Multiphasic kinetics thus suggest the presence of an extra electron donor (analogous to CuA). We observe such kinetics exclusively with cytochrome bo3 that contains a single equivalent of bound ubiquinone-8, whereas we find no bound ubiquinone in an enzyme exhibiting monophasic kinetics. Reconstitution with ubiquinone-8 converts the reaction kinetics from monophasic to multiphasic. We conclude that a single bound ubiquinone molecule in cytochrome bo3 is capable of fast rereduction of heme b and that the reaction with O2 is quite similar in quinol and cytochrome c oxidases.

Bacterial Proteins↗

PubMed2000

c-fos expression and redox state of cytochrome oxidase of rat brain in hypoxia.

Hypoxic induction of c-fos was studied in rat brains as a function of the cerebral oxygenation state using near-infrared spectroscopy by which the hemoglobin oxygenation state and redox state of mitochondrial cytochrome oxidase could be monitored noninvasively. Following reoxygenation after hypoxia, the expression of c-fos and MAP2 mRNAs was followed by reverse transcription-coupled PCR. The expression of MAP2 remained unchanged throughout all the conditions from 21 to 8% FiO2. Under mildly hypoxia conditions, c-fos mRNA was not induced. Hemoglobin was partially deoxygenated but cytochrome oxidase remained fully oxidized. Severe hypoxia, where cytochrome oxidase was reduced, caused a significant induction of c-fos mRNA At this stage, the oxygen concentration in cerebral tissue fell to < 10(-7) M. These data suggest that the decline in oxidative phosphorylation might be a trigger for the induction of c-fos mRNA.

Animals↗

PubMed1983

Cytochrome oxidase subunit 2 gene in Neurospora crassa mitochondria.

The nucleotide sequence of the cytochrome oxidase subunit 2 (COX2) gene has been obtained from cloned mitochondrial DNA segments of Neurospora crassa. The coding sequences have been identified on the basis of protein sequence homology with the subunit 2 of cytochrome oxidase from yeast and man. The postulated precursor of the N. crassa subunit 2 protein is 250 amino acids long, with a molecular weight of 28,700. As in the tRNA and rRNA genes, the subunit 2 gene is flanked by G + C-rich palindromic sequences, which are highly conserved in N. crassa mitochondria. Three major transcripts have been detected by Northern blot hybridization. A transcript of 1100 bases is tentatively considered the fully processed mRNA. Furthermore, S1 nuclease protection experiments have revealed that the putative subunit 2 mRNA has a 330 nucleotide long 5' leader sequence.

Amino Acid Sequence↗

PubMed1989

Microphotometric study on cytochrome oxidase and lactate dehydrogenase activities in mouse spermatozoa during maturation and in vivo and in vitro capacitation.

In Eutherian (mammalian) spermatozoa, maturation and capacitation are associated to modifications of the metabolic activities. In order to demonstrate such variations, a quantitative cytochemical study was carried out on cytochrome oxidase and L-lactate dehydrogenase activities in mouse spermatozoa collected from the male and female genital tracts and at different times of the in vitro capacitation. Microdensitometric measurements were made on a Vickers M85 integrator microdensitometer at lambda = 480 +/- 5 nm and lambda = 585 +/- 5 nm wavelengths for the cytochrome oxidase and LDH activities, respectively. The cytochrome oxidase activity first decreases and then increases significantly both during maturation and during capacitation in vivo and in vitro. The LDH activity decreases significantly and gradually in the male and female genital tracts as well as in the course of in vitro capacitation where, however, an enhancement in the anaerobic glycolysis occurs.

Animals↗

PubMedDate not supplied

[Ultracytochemical heterogeneity of cytochrome oxidase activity in rat cardiomyocytes].

Optimum conditions are developed for ultracytochemical detection of cytochrome oxidase in cardiomyocytes from the rat heart ventricles. Conditions mentioned above rest on using of o-dianisidine and double contrasting of microscopic sections by uranyl and lead acetates. Data from studies in heterogeneity of cytochrome oxidase activity as dependent on the structural-functional state (electronic density) of myocardium cells are presented.

Animals↗

PubMed2002

Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase.

COX19, a nuclear gene of Saccharomyces cerevisiae, was cloned by transformation of a respiratory-deficient mutant from complementation group G188 of a pet mutant collection. The gene codes for an 11-kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesize the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA center of subunit 2 of cytochrome oxidase. The similarity in their subcellular distribution, combined with the presence of four cysteines in Cox19p that align with a subset of the cysteines in Cox17p, suggests that like the latter, Cox19p may function in metal transport to mitochondria.

Amino Acid Sequence↗

PubMed1978

Changes in leucocyte cytochrome oxidase activity associated with deficiency of copper in laboratory and farm animals.

The cytochrome oxidase activity of circulating leucocytes was investigated by means of a semiquantitative method using blood films. A significant decrease in activity was found in male rats, cattle and sheep that had been deprived of copper. During copper depletion, leucocyte cytochrome oxidase activity declined more slowly than did plasma copper concentration and plasma ferroxidase I activity, and so was less sensitive as a guide to the copper status of the animal.

Animals↗

PubMed1994

Quantitative mapping of cytochrome oxidase activity in the central auditory system of the gerbil: a study with calibrated activity standards and metal-intensified histochemistry.

The objective was to obtain detailed topographic determinations of cytochrome oxidase activity in the gerbil central auditory system at the light microscopic level. Quantitative techniques were developed using (1) tissue standards calibrated to express histochemical measures as actual enzyme activity units, (2) densitometry and image analysis of histochemical reaction product formation, (3) spectrophotometry of cytochrome oxidase activity, and (4) a cobalt-intensified staining procedure compatible with autoradiography and other techniques requiring fresh-frozen brains without perfusion-fixation. Linear relationships between incubation time, section thickness, and activity of dissected brain regions, with their reaction product measured densitometrically were determined. Auditory structures with the high activities showed about 8 times the labeling intensity of the white matter or control sections inhibited with cyanide, glutaraldehyde, or heat. This indicated the high sensitivity of the method without loss of specificity. Specific activity for each of the 18 auditory structures measured were all above the units measured for whole brain homogenates, supporting the notion that basal levels of oxidative metabolism are greater for the auditory system. There was a progressive decrement in activity from brain stem to forebrain auditory structures. The more peripheral nuclei also showed a higher proportion of somatic as compared to neuropil reactivity. In contrast, auditory midbrain and thalamocortical regions were characterized primarily by neuropil reactivity. Comparison of intrinsic patterns of activity with morphological schemes to subdivide nuclei, showed a good correspondence with classical subdivisions derived from Golgi studies. The reported activities may provide a base of normative data in the gerbil for subsequent studies of central auditory functions. The method presented fulfilled established quantitative criteria and provided a more sensitive approach for regional mapping studies of brain cytochrome oxidase activity.

Animals↗

PubMed1993

Thyroxine-induced changes in metabolic rate and cytochrome oxidase activity in Thamnophis sirtalis: effects of nutritional status.

The effects of nutritional status on thyroxine-induced changes in standard metabolic rate (SMR), and the activity of hepatic cytochrome oxidase were examined in the garter snake Thamnophis sirtalis. Twelve snakes were fed ad libitum, and 12 more were fed a maintenance diet, which was half as many fish per gram of body weight as that eaten by ad libitum snakes. Snakes in the first group gained weight during the 3-week treatment, while individual snakes in the second group either maintained their original weight or showed a slight loss (less than 10%). Within each diet treatment, half of the snakes received a 5-mg thyroxine (T4) pellet implant, and half received placebo implants. Plasma [T4] was unchanged by treatment. Plasma [T3] was elevated in T4-supplemented snakes fed ad libitum, but the difference was not statistically significant (P = 0.09). Standard metabolic rate and cytochrome oxidase activity at 25 degrees were increased significantly (34 and 24%, respectively) only in the T4-supplemented snakes on the ad libitum diet. Thus, T. sirtalis must be in a positive energy balance for thyroid hormones to have an effect on SMR or hepatic cytochrome oxidase activity.

Animals↗

PubMed1990

Use of oxonol V as a probe of membrane potential in proteoliposomes containing cytochrome oxidase in the submitochondrial orientation.

Absorbance changes in the anionic dye bis[3-phenyl-5-oxoisoxazol-4-yl]pentamethineoxonol (oxonol V) can be used to monitor the membrane potential of liposomes and cytochrome c containing cytochrome oxidase proteoliposomes (c-loaded COV). Diffusion potentials (positive inside the vesicles) cause an increase in the dye extinction, with a maximum at 640 nm. A similar increase is seen upon energization of internally facing cytochrome oxidase molecules in c-loaded COV. Both "passive" and "active" responses are only seen when the dye is fully bound to the vesicle membrane. Calibration curves using potassium or n-butyltriphenylphosphonium ion (BTPP+) diffusion potentials are linear up to 100 mV and pass through the origin. Diffusion potentials (positive inside) also cause an increase and red shift in the oxonol V fluorescence emission spectrum. However, potentials of the same sign induced by cytochrome oxidase turnover induce a large fluorescence quenching in c-loaded COV. A similar anomaly has been observed with submitochondrial particles [Smith, J. C., Russ, P., Cooperman, B. S., & Chance, B. (1976) Biochemistry 15, 5094-5105]. A model is proposed consistent with these responses. It is suggested that the dye molecules move further into the membrane phase upon energization, causing the absorbance increase. In the presence of active enzyme, anionic dye molecules are attracted to a positive dipole on each enzyme molecule, causing self-quenching of the fluorescence.

Calibration↗

PubMed1997

Submitochondrial distributions and stabilities of subunits 4, 5, and 6 of yeast cytochrome oxidase in assembly defective mutants.

The concentration and submitochondrial distribution of the subunit polypeptides of cytochrome oxidase have been studied in wild type yeast and in different mutants impaired in assembly of this respiratory complex. All the subunit polypeptides of the enzyme are associated with mitochondrial membranes of wild type cells, except for a small fraction of subunits 4 and 6 that is recovered in the soluble protein fraction of mitochondria. Cytochrome oxidase mutants consistently display a severe reduction in the steady-state concentration of subunit 1 due to its increased turnover. As a consequence, most of subunit 4, which normally is associated with subunit 1, is found in the soluble fraction. A similar shift from membrane-bound to soluble subunit 6 is seen in mutants blocked in expression of subunit 5a. In contrast, null mutations in COX6 coding for subunit 6 promote loss of subunit 5a. The absence of subunit 5a in the cox6 mutant is the result of proteolytic degradation rather than regulation of its expression by subunit 6. The possible role of the ATP-dependent proteases Rca1p and Afg3p in proteolysis of subunits 1 and 5a has been assessed in strains with combined mutations in COX6, RCA1, and/or AFG3. Immunochemical assays indicate that another protease(s) must be responsible for most of the proteolytic loss of these proteins.

Adenosine Triphosphatases↗

PubMed1988

Increased cytochrome oxidase activity of mesencephalic neurons in developing rats displaying methylmercury-induced movement and postural disorders.

Subcutaneous administration of the neurotoxin methylmercuric chloride to developing rats produced movement and postural disorders during the 4th postnatal week. Cytochrome oxidase histochemistry revealed an increase in the oxidative metabolic activity of small neurons within the magnocellular red nucleus (RMC) and the interrubral mesencephalon. A concurrent suppression of cytochrome oxidase activity in the large neurons and neuropil of RMC was apparent relative to controls. Decortication on postnatal day 3 did not alter the course of motor impairment or the cytochrome oxidase histopathology, suggesting that the role of neocortex in the pathogenesis of methylmercury-induced movement and postural disorders is minimal.

Animals↗

PubMed1975

Cytochrome oxidase and ascorbic acid in the normal and regenerating tail of the scincid lizard, Mabuya carinata. A histophysiological study.

The concentration of ascorbic acid (AA) and the histochemical distribution of this vitamin together with cytochrome oxidase have been investigated in the normal and regenerating tail of the Scincid lizard, Mabuya carinata. An interesting aspect of this investigation is the observation of a total lack of cytochrome oxidase in both the normal and regenerating tail of the lizard, except for the differentiating phase. On the other hand, AA has been found to be present in the normal and regenerating tail with above normal levels during wound healing (twofold) and differentiation (fivefold). In the light of the poor cytochrome oxidase activity, the higher content of AA noted during regeneration has been construed to play a possible role in the respiratory mechanics of the regenerating lizard tail. Further, the importance of AA in cellular metabolism and the wound healing and differentiative processes have also been discussed.

Animals↗

PubMed1993

The effect of antibodies to subunit V of cytochrome oxidase on cyanide inhibition of electron transfer.

Binding of antibodies raised against subunit V of mammalian cytochrome oxidase to the intact membranous enzyme is redox-sensitive, suggesting the existence of 'open' and 'closed' protein conformers (Freedman, J.A., Cooper, C.E., Leece, B., Nicholls, P. and Chan, S.H.P. (1988) Biochem. Cell Biol. 66, 1210-1217). Similar open and closed states for the oxygen-reacting site have been proposed to explain cyanide binding kinetics (Jensen, P., Wilson, M.T., Aasa, R. and Malmström, B.G. (1984) Biochem. J. 224, 829-837). We therefore examined cyanide inhibition of oxidase activity polarographically and spectrophotometrically using soluble oxidase preincubated with and without anti-subunit V or non-immune rabbit gamma-globulin. The subunit-specific antibody decreased the cyanide 'on' rate and essentially eliminated the rapid phase of cyanide binding. We conclude that (i), bound antibody blocks HCN binding; (ii), antibody and HCN probably bind to the same conformation of the oxidase and (iii), the 'open'-'closed' conformation change that modulates binding of HCN may be similar to that which modulates antibody binding. The results are consistent with some reciprocating models of electron transfer and energy transduction by the oxidase (cf., Wikström, M.K.F., Krab, K. and Saraste, M. (1981) Cytochrome Oxidase: A Synthesis).

Animals↗

PubMed1977

On the molecular weight of mitochondrially synthesized subunits of rat liver cytochrome oxidase.

The subunit composition of cytochrome c oxidase from rat liver mitochondria was studied by dodecylsulfate polyacrylamide gel electrophoresis. The apparent molecular weight of the seven subunits are in reasonable agreement with published data on cytochrome c oxidase subunits from other sources. Two additional subunits were found if the electrophoresis was performed with 8m urea, due to splitting of the smallest subunit. Performic acid oxidation of the isolated subunits I and II increased the apparent molecular weights from 38000 to 48000 and from 24500 to 29000, respectively, accompained by a normalization of the anomalous behaviour of subunit I in the Ferguson plot. It is suggested that performic acid, by splitting extremely inaccessible disulfide bridges, mediates full complexing of the subunits by dodecylsulfate, thus permitting the determination of the real molecular weights by dodecylsulfate polyacrylamide gel electrophoresis.

Animals↗