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PubMed1989

The effect of pH changes on the optical spectrum of oxidised cytochrome oxidase.

The sensitivity to pH changes of oxidised cytochrome oxidase, oxidised oxidase-cyanide and oxidase-azide complexes was investigated by optical difference spectroscopy in the pH region 6.0-8.2. The responses of the optical spectrum of oxidised oxidase and the oxidase-cyanide complex are almost fully developed within some minutes after a pH change of 1-2 units. A blue shift of the spectrum of oxidised oxidase and the oxidase-cyanide complex is observed with decreasing pH, whereas the oxidase-azide complex is almost insensitive to the pH change. From the pH insensitivity of the oxidase-azide complex and the differences in the pH-induced spectral changes of the oxidase-cyanide complex relative to unliganded oxidase, it is concluded that the spectral pH sensitivity in the oxidised enzyme is probably associated with proton binding at or near cytochrome a3 only. Similar absorption changes are observed with the oxidised oxidase on increasing the pH and on the binding of azide to oxidised oxidase at constant pH. It is suggested that azide binding is probably associated with the deprotonation of some ionizable group(s) in the vicinity of the cytochrome a3-CuB site.

Animals↗
PubMed2005

Changes in cytochrome oxidase in the piriform cortex after status epilepticus in adult rats.

PURPOSE: The piriform cortex is involved in genesis and propagation of temporal lobe seizures. Degenerating neurons demonstrated by FluoroJade B staining are visible early after status epilepticus (SE) as well as after longer intervals. Furthermore, the piriform cortex is activated during an early phase of experimental temporal seizures, as described by magnetic resonance imaging (MRI) studies. It indicates that the early activity of the piriform cortex should be accompanied by increased adenosine triphosphate (ATP) production. Cytochrome oxidase activity in the brain may be used as an endogenous metabolic marker for neurons. The present research studied activity of the cytochrome oxidase separately in the rostral and caudal parts of the piriform cortex after lithium chloride-pilocarpine-induced SE in adult rats. METHODS: SE was induced by a single dose of pilocarpine (40 mg/kg) in LiCl-pretreated adult Wistar rats. Cytochrome oxidase activity was mapped by optical density on sections stained with histochemistry separately in the rostral and caudal parts of the piriform cortex. RESULTS: Optical density of the rostral part of the piriform cortex remained nearly unchanged at both 1 week (0.284 +/- 0.009 in SE group vs. 0.297 +/- 0.005 in controls) and 3 months (0.318 +/- 0.007 in SE group vs. 0.333 +/- 0.004 in controls) after SE intervals. The caudal part of the piriform cortex showed a decrease of optical density in both groups at 1 week (0.265 +/- 0.007 in SE group vs. 0.285 +/- 0.009 in controls) and 3 months after SE (0.292 +/- 0.006 in SE animals vs. 0.310 +/- 0.003 in controls), respectively. Nissl-stained sections demonstrated a marked neuronal loss and gliosis and/or necrotic cavities through the caudal piriform cortex 1 week after SE. CONCLUSIONS: Our results demonstrated that damage of the piriform cortex is not homogeneous and thus that its parts are differently involved in epileptic activity.

Animals↗
PubMedDate not supplied

Three-dimensional reconstruction of cytochrome oxidase vesicle crystals prepared by cholate solubilization.

Cytochrome oxidase vesicle crystals with long-range order have been obtained from cholate-solubilized, highly purified reconstitutively active preparations. These crystals, which are suitable for electron-microscopic structure investigation, show pgg symmetry in the 0 degree projection. Using Fourier reconstruction and modified back-projection methods, a three-dimensional reconstruction has been obtained at a resolution of 25 A. Our structural results are in agreement with the model of Henderson et al. [J. Mol. Biol. 112, 631 (1977)] obtained for their Triton-derived crystals.

Cholic Acid↗
PubMed2003

Molecular analysis of the biting midges (Diptera: Ceratopogonidae), based on mitochondrial cytochrome oxidase subunit 2.

Sequences from the mitochondrial cytochrome oxidase subunit 2 gene (cox2) were determined for 14 species from the family Ceratopogonidae, representing 12 genera and all five subfamilies, along with six representatives of other nematoceran families. The purpose was to develop a molecular phylogeny of the Ceratopogonidae, and interpret the phylogenetic position of the family within the infraorder Culicomorpha. These taxa have been analysed using cladistic methodology which, in combination with an excellent fossil record, provides a well established morphological phylogeny. Sequence analysis of cox2 revealed a high degree of sequence divergence among the species, reflecting in part the antiquity of the family, but also a significant acceleration of sequence evolution in the ceratopogonids compared to other nematoceran Diptera. Phylogenetic reconstruction by neighbor-joining and maximum parsimony gave strong support for an early separation of an ancient lineage that includes the two genera, Austroconops and Leptoconops, from the remainder of the family. The results support the existence of a clade that includes two subfamilies, Dasyheleinae and Forcipomyiinae, and this clade appears as sister to the remaining subfamily, Ceratopogoninae. The molecular phylogeny also supports monophyly of the Ceratopogonidae, and either a sister or paraphyletic relationship of this family with the Chironomidae.

Animals↗
PubMed1988

Increased cytochrome oxidase activity in alkali-burned corneas.

Cytochrome oxidase (CO) activity on alkali-burned rabbit corneas was investigated histochemically to determine the metabolic change in inflamed corneas during wound healing. Cryostat sections of chemically burned and mechanically scraped corneas were stained for CO activity, which is regarded as an index of metabolic activity. Following chemical injury, positive CO activity was detected initially in the vascular endothelial cells of limbal blood vessels. Numerous active polymorphonuclear leukocytes (PMNs) and monocytes were found intravascularly and perivascularly. Fibroblasts that appeared at the wound site exhibited marked CO activity around the limbus. Over a period of 13 days, PMNs gradually invaded the central cornea, followed by fibroblasts of high metabolic activity. The areas of PMN infiltration were the same areas in which fibroblasts showed intense staining, suggesting that a PMN-derived mediator or secondary products might affect the activation of fibroblasts. Epithelial resurfacing was delayed in the chemically burned corneas, although reepithelialization was completed within two to three days in the scraped corneas. Limbal epithelial cells, which recently were suggested as the source of epithelial renewal, showed a remarkable increase of metabolic activity in response to chemical inflammatory stimulation, whereas those in the scraped model did not. This suggests that epithelial cell renewal at the limbus was accelerated in the presence of disturbed reepithelialization.

Alkalies↗
PubMed1977

Studies of human malignant lymphomas after treatment with endoxan. I. Cytochemical studies in the respiratory enzymes succinic dehydrogenase and cytochrome oxidase.

The respiratory enzymes succinic dehydrogenase and cytochrome oxidase were studied in normal lymph node and malignant lymphoma cells under the effect of endoxan treatment. It is concluded that the decrease in the respiratory enzymes in lymphoma cells may be taken as one of the outstanding differences between the neoplastic and normal tissues.

Cyclophosphamide↗
PubMed1984

The identity of pulsed cytochrome oxidase.

Reduction and reoxidation of beef heart cytochrome oxidase, under conditions that ensure the strict absence of hydrogen peroxide, produce a fully oxidized form of the enzyme that has the Soret band at 420 nm, as opposed to the 428 nm band normally associated with the pulsed or oxygenated enzyme. The 420 nm form shows the enhancement of catalytic activity associated with the pulsed enzyme. Addition of hydrogen peroxide to the 420 nm form gives rise to the 428 nm band of the oxygenated enzyme, thereby clearly establishing that the 428 nm form is a peroxide derivative of the fully oxidized enzyme. Previous data from other groups are re-evaluated in the light of our experiments.

Animals↗
PubMed1994

Transcription and editing of cytochrome oxidase II RNAs in Trypanosoma cruzi.

The cytochrome oxidase subunit II (COII) gene is one of the maxicircle cryptogenes of kinetoplastids whose primary transcripts are sometimes modified by RNA editing to produce mature mRNAs. We determined the sequence of the COII gene in three strains of Trypanosoma cruzi (Y, Corpus Christi, and Tulahuén) and examined its developmental expression. Comparison of the RNA and DNA sequences encoding COII indicated that in the three strains of T. cruzi, four uridines are inserted in the pre-mRNA at the same positions as they are in the COII pre-mRNAs of Trypanosoma brucei, Leishmania tarentolae, and Crithidia fasciculata. The putative guide RNA (gRNA) sequence that serves as a template for the four uridine insertions is located in the 3'-untranslated region of the T. cruzi COII mRNA. Analysis of editing intermediates demonstrates that the COII gRNA remains attached to the pre-mRNA while participating in the formation of chimeric RNAs. Northern blots used to investigate stage-specific expression of the COII gene revealed RNAs of 800 and 900 nucleotides, similar in size to those present in T. brucei. In contrast to the differential expression observed in T. brucei, no difference occurs between the COII mRNA levels of insect and mammalian stages of T. cruzi.

Amino Acid Sequence↗
PubMedDate not supplied

Cytochrome oxidase and lactate dehydrogenase activities in peroxidized rabbit epididymal spermatozoa.

We report a quantitative cytochemical study on cytochrome oxidase and lactate dehydrogenase activities on rabbit epididymal spermatozoa during spontaneous lipid peroxidation. Our data show that during aerobic incubation both in NTP and KTP media the sperm cytochrome oxidase activity undergoes a significant decrease. The lactate dehydrogenase activity shows different cytochemical patterns in comparison between the two media considered. Such activity significantly increases in rabbit spermatozoa suspended in NTP medium from the first until the sixteenth hour of incubation time. At the following times the lactate dehydrogenase activity significantly declines showing yet until the later times of incubation integrated optical density values fairly high. During the whole period of the aerobic incubation, the spermatozoa suspended in medium KTP show lactate dehydrogenase integrated optical density values which not significantly differ from those of the control in spite of an initial enhancement from the first until the thirteenth hour of the experimental treatment.

Animals↗
PubMed1989

Cytochrome oxidase patches and Meynert cells in monkey visual cortex.

In area 17 of Macaca mulatta large Meynert cells have their cell bodies located in the vicinity of the border between layers V and VI. When the distribution of these cell bodies is plotted in the tangential plane they are found not to be randomly distributed, but arranged in a sheet such that they outline holes or gaps. In sections of area 17 reacted for cytochrome oxidase, which indicates the relative level of metabolic activity in neurons and neuropil. Meynert cell bodies are clearly visible as large highly reactive neurons against a background of much lower reactivity. In reconstructions it is apparent that the holes or gaps in their distribution pattern lie beneath the high cytochrome oxidase reactive patches or blobs in layer II/III. In other words, the Meynert cell bodies lie predominantly beneath the low cytochrome oxidase reactive interpatch regions of layer II/III. On the basis of what is known about the functional connections of neurons in area 17 it is suggested that this arrangement of Meynert cells indicates that they are involved in the detection of movement in the visual field, a suggestion that is supported by the known projections of the Meynert cells to the superior colliculus and cortical area V5.

Animals↗
PubMed1991

Dissociative effects of ibotenic and quisqualic acid-induced basal forebrain lesions on cortical acetylcholinesterase-positive fiber density and cytochrome oxidase activity.

The behavioral effects of excitatory amino acid-induced basal forebrain lesions have been conventionally attributed to the loss of cholinergic neurons innervating cortical areas. However, comparative examinations of quisqualic acid- and ibotenic acid-induced lesions to this region have suggested that the behavioral consequences of ibotenate-induced lesions may not be exclusively related to the loss of cholinergic neurons [Etherington R. et al. (1987) Neurosci. Res. Commun. 1, 135-143; Robbins T. W. et al. (1989) Neuroscience 28, 337-352]. These findings prompted the present investigation of the effects of quisqualic acid- and ibotenic acid-induced basal forebrain lesions on cortical cholinergic fiber density and cytochrome oxidase activity. Parallel brain sections from rats with unilateral lesions produced by each toxin were examined for cytochrome oxidase activity and acetylcholinesterase-positive fiber density, at a period of four, eight and 20 days postlesion. Quisqualic acid-induced lesions resulted in a greater loss of cortical acetylcholinesterase-positive fibers than did ibotenic acid-induced lesions, but the latter lesions produced a greater reduction in cytochrome oxidase activity. These results suggest that the loss of cortical cholinergic afferents does not contribute to the cortical metabolic decrease induced by infusions of ibotenic acid into the basal forebrain. Thus, the behavioral and metabolic consequences of ibotenic acid-induced lesions may be due to the destruction of an additional, noncholinergic pathway.

Acetylcholinesterase↗
PubMed1992

Changes in activity of cytochrome oxidase in the cochleae of guinea pigs with experimental endolymphatic hydrops.

Cochlear dysfunction may indicate inadequate generation of intracellular metabolic energy which is necessary for the regulation of the transport of ions and fluid as well as production of electro-energy in the cochlea. Changes in cochlear function in the early stages of endolymphatic hydrops attributed to dysfunction of the sensory hair cells and stria vascularis were investigated. The main source of metabolic energy, produced by intracellular respiration, is located in the stria vascularis and sensory hair cells. Since cytochrome oxidase is one of the most important respiratory enzymes, vibratome sections of hydropic and normal cochleae were stained cytochemically for cytochrome oxidase activity in this study. Decreased activity of this enzyme was consistently shown in the normal-appearing outer hair cells and stria vascularis, as well as the degenerated hair cells and stria vascularis, of the higher turns of the hydropic cochlea. The results coincide with those in other studies of electrophysiologic changes in cochlear function in hydropic animals. A decrease in the activity of respiratory enzymes was noted before the destruction of the cellular structures. The activity of cytochrome oxidase may serve as a useful indicator for demonstrating the functional status of cochlear hair cells and stria vascularis.

Animals↗
PubMedDate not supplied

Electron microscopic cytochemistry of cytochrome oxidase activity in the conduction system of the canine heart.

Histochemistry and electron microscopic cytochemistry of cytochrome oxidase in the conduction system were studied with the 3,3'-diaminobenzidine (DAB) method in adult canine hearts. This enzyme was distinctly less active in the entire conduction system than in the working myocardium. By electron microscopy, enzymatic activity per cristal membrane was apparently similar in both specialized and working cardiocytes. However, the volume fraction of cell occupied by mitochondria and the density of cristal membranes in mitochondria were smaller in the specialized cells in the sinus node, atrioventricular (AV) node, His bundle, and Purkinje fibers. These observations define the nature of decreased histochemical activity of cytochrome oxidase in cells of the conduction system, which is caused entirely by the decrease in activity per unit of mitochondrial volume and unit of cell volume in the specialized cardiac tissues.

Animals↗
PubMed1995

The reaction of cyanide with peroxidatic forms of cytochrome oxidase.

The interaction of peroxidatic derivatives of cytochrome c oxidase with cyanide has been investigated by optical spectroscopy and the stopped-flow method. Two reactions were found in the conversion of peroxy cytochrome oxidase to its cyanide complex. The first reaction is characterized by the loss of the 607 nm band, an increase in absorbance at 655 nm, and a decrease in absorbance at 432 nm resulting from a blue-shift of the Soret band; this reaction occurred with a bimolecular rate constant of about 90 M-1 s-1. The second reaction is observed as an absorbance increase at 585 and 432 nm; the latter was due to a red-shift of the Soret band. This second process proceeded with a rate constant of about 22 M-1 s-1. Both reaction rates are linearly dependent on the concentration of cyanide between 5 and 100 mM. The reappearance of the 655 nm band at the completion of the first reaction suggests that cytochrome a3 becomes transiently high-spin, a finding which implies that cyanide is not initially bound to this heme center. It appears that preparations of oxidized CcO contain small but variable amounts of the peroxy form. The variable content of this form is probably responsible for the different response of oxidized oxidase to low concentrations of cyanide [Berka, V., Vygodina, T., Musatov, A., Nicholls, P., & Konstantinov, A. A. (1993) FEBS Lett. 315, 237-241] and may explain the biphasic reduction of the binuclear center with dithionite [Cooper, C. E., Junemann, S., Ioannidis, N., & Wrigglesworth, J. M. (1993) Biochim. Biophys. Acta 1144, 149-160].

Cyanides↗
PubMed1994

Rescue of a maize mitochondrial cytochrome oxidase mutant by tissue culture.

The maize NCS6 mitochondrial mutation is a partial deletion of the cytochrome oxidase subunit 2 gene (cox2) that survives heteroplasmically in the plant. Mutant mitochondria segregate from normal mitochondria during somatic development giving rise to defective sectors on the plants, including areas of kernel abortion on the ears. Embryos from NCS6 kernels can be rescued by tissue culture. Slowly growing Type II callus derived from one of these embryos has been shown by PCR analysis to be homoplasmic for the mutation, carrying only the defective mitochondrial cox2 gene. Most of the rescued embryos were heteroplasmic for normal and mutant genes and heteroplasmy was maintained in the callus cultures. However, when suspension cultures were initiated from heteroplasmic calli, normal cells were shown to have a selective advantage. When the homoplasmic cox2 mutant callus cultures were placed on regeneration medium, plantlets did not regenerate. Heteroplasmic calli were capable of regeneration under the same conditions. These studies suggest that the functioning of mitochondrial cytochrome oxidase is not essential for growth as callus, but is required for the differentiation and development of plants.

Base Sequence↗
PubMed1988

Electron redistribution in mixed valence cytochrome oxidase following photolysis of carboxy-oxidase.

Absorbance changes at 446 nm in purified cytochrome oxidase following flash photolysis of carboxy-oxidase poised in the mixed valance state at +220 mV show biphasic kinetics. One phase corresponds to CO recombination to ferrous cytochrome a3 with an energy of activation of 9 kcal/mol; the second phase is 3-5 times faster with an energy of activation of 9.15 kcal/mol. Following flash photolysis at approximately -60 degrees C, cytochromes a and c and the 840-nm CuA species are observed to undergo reduction as electrons from ferrous unliganded cytochrome a3 equilibrate with the equipotential redox centers of the oxidase; as CO recombines with ferrous cyochrome a3, these centers are oxidized and the mixed valence carboxy-oxidase is regenerated. Electron redistribution between centers of the oxidase in the forward and reverse directions occurs faster than does the binding of CO.

Animals↗
PubMed2000

Unaltered cytochrome oxidase, glutamate dehydrogenase and glutaminase activities in platelets from patients with sporadic amyotrophic lateral sclerosis--a study of potential pathogenetic mechanisms in neurodegenerative diseases.

Sporadic Amyotrophic Lateral Sclerosis (SALS) is a fatal neurologic disease characterized by degeneration of motor neurons in the spinal cord, brainstem and cortex. While familial cases of ALS exist, the sporadic form accounts for the majority of adult-onset cases. It has been hypothesized that the neurodegenerative mechanisms underlying SALS might arise from glutamate-mediated excitotoxicity and mitochondrial dysfunction. Studies on autopsied SALS spinal cord and brain have reported decreased cytochrome oxidase activity, decreased astrocytic glutamate-transporter protein, and alterations of glutamate levels and glutamate metabolizing enzyme activities. We conjectured that if alterations in glutamate metabolism and cytochrome oxidase activity occur in the SALS central nervous system these alterations may also be manifested in peripheral tissues such as platelets in living SALS patients. In this study we compared the activities of cytochrome oxidase, citrate synthase, glutamate dehydrogenase and glutaminase in platelets from SALS and control subjects. We found that there were no differences in any of the enzyme activities measured between the two groups. Our data argue against generalized ubiquitous biochemical alterations of these enzymes in SALS patients.

Blood Platelets↗