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PubMed1987

Principles of coupling between electron transfer and proton translocation with special reference to proton-translocation mechanisms in cytochrome oxidase.

The recent general acceptance of the proton-pumping function of cytochrome oxidase has stimulated discussion and experiment on possible underlying molecular mechanisms. Adequate experimental design requires clear understanding of the theoretical principles governing such a linked function. The increasing structural knowledge of cytochrome oxidase also contributes to a present-day requirement of more precise chemical and physical description of redox-linked proton translocation, which is the fundamental process underlying conservation of energy from aerobic metabolism in all eukaryotes and many bacteria. This essay is based on our original theoretical treatment of this problem, which is expanded here to include discussion of more recent analyses by others, classification of different types of coupling principles, as well as some concrete proposed molecular mechanisms. The latter will be analysed qualitatively, and in some cases quantitatively where this is possible, using a common theoretical framework to help comparison between models. Experimental findings relevant to this problem will be critically reviewed, and some suggestions will be made to stimulate further experiments dedicated to clarify the problem.

Biological Transport↗
PubMed1986

Laminar distribution and patchiness of cytochrome oxidase in mouse superior colliculus.

The cytochrome oxidase (CO), acetylcholinesterase (AChE), myelin, and Nissl stains were studied and compared to develop an anatomical system identifying the laminar architecture of the mouse superior colliculus. The CO and myelin stains are shown to define collicular laminae more distinctly than does the Nissl stain. The layer of large rostrocaudally coursing fiber bundles that has formerly been referred to in the rodent literature as stratum album intermediale (SAI; layer V) is renamed as a sublayer of the stratum griseum intermediale (SGI; layer IV) to conform with the nomenclature for the cat superior colliculus of Kaneseki and Sprague ('74, J. Comp. Neurol. 158:319-338). Patches of CO activity in layer IV (SGI) are shown that contain intensely stained, large, multipolar cell bodies. The CO patches do not correspond to those previously reported for AChE. The CO, myelin, and AChE stains all indicate the presence of a large lateral extension termed the flank of layer IV (SGI). In contrast to the classical lamination pattern of the superior colliculus, the flank has no overlying layer II (stratum griseum superficiale, SGS) or layer III (stratum opticum, SO).

Acetylcholinesterase↗
PubMed1986

Laminar and cellular localization of cytochrome oxidase in the cat striate cortex.

Cytochrome oxidase (C.O.) was histochemically localized in the cat striate cortex at the light and electron microscopic levels. The results indicate that the oxidative metabolic activity within the cat striate cortex may vary between (1) different laminae, (2) neurons and glia, (3) different neuron types, (4) dendrite and soma of the same cell, (5) different types of dendrites, (6) different segments of the same dendrite, and (7) different classes of symmetric and asymmetric axon terminals. Maximal laminar C.O. staining was localized within geniculoreceptive layer IV. Darkly reactive neurons include the large (presumed corticotectal) pyramids of layer V, and various classes of large and medium-sized presumed GABAergic nonpyramidal cells sparsely distributed throughout layers II-VI. The small and medium-sized pyramids of layers II, III, V, and VI, as well as many of the smaller presumed GABAergic neurons, were only lightly or moderately reactive. The darkly reactive neurons tended to be those that received convergent or proximally localized asymmetric axosomatic synapses, implying that they are strongly driven by excitatory synaptic input. The darkly reactive nonpyramids resembled those that form GAD+, symmetric axosomatic synapses with pyramidal cells. The dark reactivity of the symmetric synaptic terminals indicates that they mediate strong inhibition of neuronal discharge. The dark reactivity of a class of large asymmetric terminals in layer IV is likely to represent highly active geniculocortical terminals. The predominant distribution of elevated C.O. reactivity in dendrites is correlated with reported sites of (1) convergent excitatory synaptic input, (2) maximal field potentials, (3) highly active ion transport, and (4) Na+, K+-ATPase.

Animals↗
PubMed1995

Distribution of brain cytochrome oxidase activity in various neurodegenerative diseases.

Cytochrome oxidase (CO) is the terminal complex of the mitochondrial respiratory chain which generates ATP by oxidative phosphorylation. We have measured CO activity in six different brain regions of patients with senile dementia of Alzheimer type (SDAT, n = 10), presenile dementia of Alzheimer type (PDAT, n = 10), Lewy body dementia with SDAT (LBD, n = 5), cerebrovascular dementia (CVD, n = 10), Parkinson dementia (PD, n = 5), and in controls (n = 8), as all confirmed by neuropathological evaluation. CO activity was lower in the frontal and parietal cortex of SDAT patients compared to controls. Patients with PDAT, LBD, CVD or PD showed no significant reduction of the enzymatic activity in the six regions studied. Our results show that reduced CO activity might play a role in the physiopathology of senile dementia of Alzheimer type.

Aged↗
PubMed2001

Effects of learning on cytochrome oxidase activity in cuttlefish brain.

Using cytochrome oxidase (CO) histochemistry, the effects of instrumental conditioning in cuttlefish central nervous system were examined. The posterior superior frontal lobe showed an increase of CO labelling just after training, whereas the anterior superior frontal lobe exhibited a decrease of CO staining 24 h post-training. These findings provide the first metabolic evidence for the involvement of the superior frontal lobe in learning and memory processes in cuttlefish. It is concluded that CO histochemistry can be used to provide a functional mapping of learning-induced plasticity in cuttlefish brain.

Animals↗
PubMed1991

A fresh mount method for cytochrome oxidase histochemistry.

A simple modification of cytochrome oxidase histochemistry was undertaken to prevent the artifactual condensation of reaction product. The quality and reliability of the histochemical method were greatly improved by using fresh mounted tissue [corrected].

Animals↗
PubMed1985

The first twelve amino acids of a yeast mitochondrial outer membrane protein can direct a nuclear-coded cytochrome oxidase subunit to the mitochondrial inner membrane.

We have used an in vivo complementation assay to test whether a given polypeptide sequence can direct an attached protein to the mitochondrial inner membrane. The host is a previously described yeast deletion mutant that lacks cytochrome oxidase subunit IV (an imported protein) and, thus neither assembles cytochrome oxidase in its mitochondrial inner membrane nor grows on the non-fermentable carbon source, glycerol. Growth on glycerol and cytochrome oxidase assembly are restored to the mutant if it is transformed with the gene encoding authentic subunit IV precursor, a protein carrying a 25-residue transient pre-sequence. No restoration is seen with a plasmid encoding a subunit IV precursor whose pre-sequence has been shortened to seven residues. Partial, but significant restoration is achieved by an artificial subunit IV precursor in which the authentic pre-sequence has been replaced by the first 12 amino acids of a 70-kd protein of the mitochondrial outer membrane. If this dodecapeptide is fused to the amino terminus of mouse dihydrofolate reductase (a cytosolic protein), the resulting fusion protein is imported into the matrix of yeast mitochondria in vitro and in vivo. Import in vitro requires an energized inner membrane. We conclude that the extreme amino terminus of the 70-kd outer membrane protein can direct an attached protein across the mitochondrial inner membrane.

Biological Transport↗
PubMed1980

Characterization of the intermediates in the reaction of mixed-valence state soluble cytochrome oxidase with oxygen at low temperatures by optical and electron-paramagnetic-resonance spectroscopy.

The reaction of soluble mixed-valence-state (a3+CuA 2+.CuB + A32+) cytochrome oxidase with O2 at low temperature was studied by optical and e.p.r. spectroscopy. The existence of three intermediates [Clore & Chance (1978) Biochem. J. 173, 799-8101] was confirmed. From the e.p.r data it is clear that cytochrome a and CuA remain in the low-spin ferric and cupric states respectively throughout the reaction. No e.p.r. signals attributable to cytochrome a3 or CuB were seen in the intermediates. The difference spectra (intermediates minus unliganded mixed-valence-state cytochrome oxidase) and absolute spectra of the three intermediates were obtained. The chemcal nature of the three intermediates is discussed in terms of their spectroscopic properties. A catalytic cycle for cytochrome oxidase is proposed.

Chemical Phenomena↗
PubMed1986

Studies on the role of the oligomeric state and subunit III of cytochrome oxidase in proton translocation.

Anion-exchange fast protein liquid chromatography in the presence of lauryldimethylamine N-oxide (LDAO) was introduced to separate cytochrome oxidase into different complexes that either did or did not contain subunit III. Both kinds of enzyme complex exhibited H+ translocation after reconstitution into phospholipid vesicles, but with a significantly (approx. 50-60%) reduced H+/e- ratio as compared with unchromatographed enzyme. The anion-exchange FPLC fractions of the enzyme (with or without subunit III) sedimented more slowly than the control enzyme upon sucrose gradient centrifugation in the presence of cholate and a high potassium phosphate concentration. When the control enzyme was subjected to the sucrose gradient centrifugation in the presence of LDAO or Triton X-100, instead of cholate, one band containing all subunits was observed, which sedimented slowly like the FPLC fractions. Transfer of this band to cholate medium, and reapplication on the sucrose gradient (with cholate), yielded both a slow- and a fast-migrating band after centrifugation. Enzyme complexes that sedimented slowly or rapidly in the sucrose gradients revealed longer and shorter elution times, respectively, in gel filtration FPLC. This suggests that these complexes corresponds to monomers and dimers of cytochrome oxidase. Solubilization of proteoliposomes and subsequent sucrose gradient centrifugation in cholate yielded one fast-migrating band for the untreated enzyme, but both a fast- and a slow-migrating band for the anion-exchange FPLC-treated enzyme, which was exclusively slow-migrating before reconstitution into liposomes. It is suggested that dimerisation of monomeric cytochrome oxidase may be favoured when the enzyme encounters a membranous milieu, and that the dimeric structure might be necessary for proton translocation.

Animals↗
PubMed1989

Modulation of cytochrome oxidase kinetics by indirect antibody action.

Polyclonal antibodies raised against isolated subunit V from beef heart cytochrome oxidase or against the intact enzyme increase its apparent affinity for the substrate cytochrome c at the high-affinity site while diminishing the turnover at that site. At the low-affinity site the major action of both types of antibody is to reduce the apparent affinity for cytochrome c. At high ionic strengths the kinetic effect of anti-subunit V is very small although it still binds to the enzyme. The results are interpreted in terms of a model for the enzyme in which antibodies can modulate cytochrome oxidase kinetics by affecting the binding of cytochrome c, even if the antibody-binding site is on a subunit not directly involved in substrate binding.

Animals↗
PubMed1985

Localization of aspartate aminotransferase and cytochrome oxidase in the cat retina.

Using immunohistochemical techniques, we demonstrate aspartate aminotransferase (AAT)-like immunoreactivity in cone pedicles and ganglion cells of the cat retina. An identical pattern was seen when we stained for cytochrome oxidase activity, a marker for neurons which have a high metabolic activity. Tetrodotoxin selectively blocked the cytochrome oxidase labeling of ganglion cells. AAT is a key enzyme in the metabolism of aspartate and glutamate and has been proposed as a marker for neurons which use aspartate/glutamate as a neurotransmitter. Due to the close correlation between AAT-like immunoreactivity and cytochrome oxidase activity, we suggest that, at least in the retina, AAT-like immunoreactivity in fact labels cells which have a high metabolic activity.

Animals↗
PubMed1986

Cytochrome oxidase status in protein-energy-deficient rats.

Effects of changes in dietary protein have been investigated on three mitochondrial enzymes, succinate dehydrogenase, isocitrate dehydrogenase and cytochrome oxidase. Weanling rats (21 days old) were fed for 30 days on (a) a commercially produced diet (CPD) containing 21.0% dietary protein and (b) a low protein-high carbohydrate diet (LPD) containing 3.47% dietary protein. Signs of protein-energy malnutrition developed in the animals having the low protein diet. The mitochondrial enzymes were assayed. Some of the experimental rats were repleted by feeding them on a protein-rich diet for 3 weeks, and the same mitochondrial enzymes were assayed. The activity of mitochondrial cytochrome oxidase, which fell to 24% of the control values during the period of deficiency, rose to 91% of the values for control rats during rehabilitation. The activities of succinate dehydrogenase and NAD+-isocitrate dehydrogenase fell to 75 and 73% of the control values, respectively, during depletion and rose to 83 and 88% during repletion in line with the general rate of recovery of the malnourished rats as reflected by the changes in the body weights during repletion. These results show that mitochondrial cytochrome oxidase is very sensitive to changes in dietary protein. Its activity drops sharply with reduction in dietary protein intake and rises rapidly, outstripping the rate of general recovery on reverting to a protein-rich diet.

Animals↗
PubMed2001

Phylogeny of the genus Chironomus (Diptera) inferred from DNA sequences of mitochondrial cytochrome b and cytochrome oxidase I.

Two mitochondrial genes, Cytochrome b (Cytb) and Cytochrome c oxidase subunit I (COI), have been used as phylogenetic markers in Chironomids. The nucleotide sequences of 685 bp from Cytb and 596 bp from COI have been determined for 36 Chironomus species from the Palearctic, or Holarctic, and Australasia. The concatenated sequence of 1281 bp from both genes was used to investigate the phylogenetic relationships among these species. The nucleotide sequence alignments were used for construction of phylogenetic trees based on maximum-parsimony and neighbor-joining methods. Both techniques produced similar phylogenies. Monophyly of the genus Chironomus is supported by a bootstrap value of 100% at the basal branch. Six clusters of species have been revealed with high bootstrap values supporting both monophyly of each cluster and the validity of the branching order within each cluster. Four species, C. circumdatus, C. nepeanensis, C. dorsalis, and C. crassiforceps, cannot be placed into any cluster. Cytological phylogenies were constructed using the same set of species, except for C. biwaprimus. These trees showed many similarities to that obtained from the mitochondrial (mt) sequence analysis, but also a number of significant differences. When compared with the tree constructed from the sequence of 23 species available for one of the globin genes, globin 2b (gb2b), there was better support for the mt tree than for the cytological trees. An intron, which varies in its occurrence and position in gb2b, was also investigated and the distribution of the introns supports the phylogenetic history of the genus Chironomus obtained with mt data. The differences observed in the cytological trees seem to be attributable more to the retention of the same chromosome banding sequence across several species, rather than convergent evolutionary events. An important question is the determination of the position of the subgenus Camptochironomus in relation to the representatives of the nominal subgenus Chironomus, since it has been suggested that this is a separate genus. The Camptochironomus species are internal to the trees and have arisen more recently than some of the species of the subgenus Chironomus, indicating that they are not sufficiently differentiated to be considered more than a subgenus.

Animals↗
PubMed2003

The redox state of cytochrome oxidase in brain in vivo: an historical perspective.

Recent evidence suggests that cytochrome oxidase is partially reduced under resting conditions in the brain. Previous data, recorded over the past 30 years from intact brain using optical methods in the visible wavelength range, are consistent with this observation. These older data, while not conclusive in themselves, support the overall conclusions. The historical perspective on the experiments and controversies illustrates a number of useful principles. The first is that new methods tend to produce new observations that may be difficult to reproduce due to the uniqueness of the instrumentation. The second is that any new and different observations cannot be assimilated without an acceptable theoretical framework and, without assimilation can have little impact. Finally, the mechanisms which might explain why cytochrome oxidase may be more reduced than previously thought are still not fully developed and, therefore, the physiological significance of such reduction is not known.

Animals↗
PubMed1983

Cytochrome oxidase subunit II gene in mitochondria of Oenothera has no intron.

The cytochrome oxidase subunit II gene has been localized in the mitochondrial genome of Oenothera berteriana and the nucleotide sequence has been determined. The coding sequence contains 777 bp and, unlike the corresponding gene in Zea mays, is not interrupted by an intron. No TGA codon is found within the open reading frame. The codon CGG, as in the maize gene, is used in place of tryptophan codons of corresponding genes in other organisms. At position 742 in the Oenothera sequence the TGG of maize is changed into a CGG codon, where Trp is conserved as the amino acid in other organisms. Homologous sequences occur more than once in the mitochondrial genome as several mitochondrial DNA species hybridize with DNA probes of the cytochrome oxidase subunit II gene.

Journal Article↗
PubMed1982

Histochemical localization of cytochrome oxidase in the hippocampus: correlation with specific neuronal types and afferent pathways.

Cytochrome oxidase was histochemically localized in the hippocampus and dentate gyrus of various species of mammals. The most intense staining was observed within stratum moleculare of areas CA1-3 and the outer molecular layer of the dentate gyrus, as well as the somatic and basal dendritic layers of CA3. These regions correspond to the synaptic terminal fields of major excitatory afferent pathways to the hippocampus. The somata of CA3 pyramidal cells and various interneurons were more intensely stained than CA1 pyramidal cells and dentate granule cells, and these levels appeared to correlate positively with their reported rates of spontaneous firing. At the electron-microscopic level, the highest concentrations of densely reactive mitochondria were localized within the distal apical dendritic profiles of principal cells (granule and pyramidal) and certain interneurons (pyramidal basket and stratum pyramidale interneurons). The specific layers in which these structures were found are known to receive intense excitatory input from the perforant pathway. High concentrations of reactive mitochondria were also observed within the somata and proximal dendrites of CA3 pyramidal cells and various interneurons, confirming our light-microscopic observations. These results demonstrated that not only can soma and dendrites of the same cell have disparate but distinct levels of cytochrome oxidase activity, but the pattern of reactivity within a neuron's apical and basal dendrites, or even within specific dendritic segments of the same dendrite can be quite different. While the levels of somatic reactivity correlate with reported levels of spontaneous and/or synaptic activity, the degree of dendritic and somatic staining appeared to be more closely related to the intensity of convergent and/or pathway-specific excitatory synaptic input.

Afferent Pathways↗