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PubMed2004

Self-organization model of cytochrome oxidase blobs and ocular dominance columns in the primary visual cortex.

There are regularly arranged blobs that contain neurons labeled by cytochrome oxidase (CO) in the supragranular layer of the primary visual cortex (V1) of monkeys and cats. This theoretical study demonstrates that CO-blob-like patterns can be reproduced based on the thermodynamic model for the activity-dependent self-organization of afferent inputs from two different groups of neurons to the supragranular layer of the visual cortex. Computer simulation based on the model shows that within a particular parameter range each blob is centered in the ocular dominance (OD) band, as observed in macaque monkeys and galagos. Furthermore, by increasing the strength of correlation in activity between inputs from the two eyes, nearby blobs merge across OD borders, as seen in the cat visual cortex. Finally, for monocular deprivation, blobs in the deprived eyes shrink as observed in monkeys and cats. For binocular deprivation, less intensely labeled blobs were reproduced, while the blob density did not change as observed in monkeys.

Algorithms↗

PubMed1998

Energy-dependent redox state of heme a + a3 and copper of cytochrome oxidase in perfused rat brain in situ.

Using the blood-free perfused rat brain, we examined the redox behavior of cytochrome oxidase of two chromophores, heme a + a3 and copper. When perfusate inflow was stopped to induce global ischemia, the reduction of heme a + a3 was triphasic, with a rapid phase, a slow phase, and a second rapid phase. In contrast, the reduction of copper was monophasic after the rapid phase of heme a + a3. The triphasic reduction of heme a + a3 was diminished by energy-depleting treatments, such as addition of an uncoupler. The time course of the reduction of copper was not affected by the energy depletion. During global ischemia the decrease in creatine phosphate nearly paralleled the reduction of heme a + a3, whereas ATP remained at the control level until approximately 60% of heme a + a3 was reduced in the rapid phase. In the slow phase, ATP started to decrease with the reduction of copper. The redox behavior of copper was similar to the slow phase of the reduction of heme a + a3 because of the higher oxygen affinity of copper than of heme a + a3. Therefore, the rapid phase of the reduction of heme a + a3 can be used as an alarm before a decrease in ATP, whereas the reduction of copper indicates a decrease in ATP under severe hypoxia. Thus the copper signal in noninvasive near-infrared spectroscopy is a useful parameter for the clinical setting.

Animals↗

PubMed1993

A survey of the auditory midbrain, thalamus and forebrain in the chicken (Gallus domesticus) with cytochrome oxidase histochemistry.

The chicken's central auditory nuclei from the inferior colliculus to field L in the forebrain were studied with cytochrome oxidase histochemistry. All stations of the ascending pathway displayed high activity levels, including the inferior colliculus, the nucleus ovoidalis of the thalamus, and field L1 to L3 and the hyperstriatum ventrale caudale which correspond to primary and secondary auditory cortex. In the inferior colliculus a moderately active external nucleus could be distinguished from a more intensely stained central and superficial nucleus. In the central nucleus there was a lateral shell displaying stronger neuropil reactivity than a central core. Unilateral cochlea removal caused no remarkable effect in tectum and thalamus. The auditory forebrain contralateral to the lesion displayed reduced CO reactivity compared with the ipsilateral side. After bilateral cochlea extirpation auditory structures still displayed higher enzyme levels than most other nuclei.

Animals↗

PubMed1984

Reduction of cytochrome oxidase by 5,10-dihydro-5-methylphenazine: kinetic parameters from rapid-scanning stopped-flow experiments.

The kinetics of the reduction of resting cytochrome oxidase and of its cyanide complex by 5,10-dihydro-5- methylphenazine (MPH) have been characterized by rapid-scan and fixed-wavelength stopped-flow spectrophotometry in the Soret, visible, and near-IR spectral regions. In this study, we focused on a form of the resting enzyme that is characterized by a Soret absorption maximum at 424 nm. These experiments complement earlier work on the reduction of a 418 nm absorbing form of the resting enzyme [ Halaka , F.G., Babcock , G. T., & Dye, J. L. (1981) J. Biol. Chem. 256, 1084-1087]. The reduction of cytochrome a is accomplished in a second-order reaction with a rate constant of 3 X 10(5) M-1 s-1. The reduction of the 830-nm absorber, Cua, is closely coupled to but lags the reduction of cytochrome a; we have resolved a rate constant of about 20 s-1 for the copper reduction. The reduction of cytochrome a proceeds with a rate constant that is nearly independent of the spectral properties of the resting enzyme and of the ligation state of cytochrome a3. The reduction of cytochrome a3 occurs by slow, intramolecular electron transfer. We have resolved two phases for this process that have rate constants of approximately 0.2 s-1 and approximately 0.02 s-1 for both the 418- and 424-nm forms of the resting enzyme. It appears, therefore, that spectroscopic heterogeneity at the cytochrome a3 site in the resting enzyme exerts very little influence on the kinetics of the anaerobic reduction of the oxidase metal centers. From this we conclude that the rate of electron transfer to the a3 site is probably controlled by the protein conformation and not primarily by local factors within the a3 environment.

Electron Transport Complex IV↗

PubMed1996

Formate bound to cytochrome oxidase can be removed by cyanide and by reduction.

Using 14C-radiolabeled formate we have found that the rapid form of oxidized cytochrome oxidase can bind up to 1 mol of formate. Treatment of this formate-ligated enzyme with excess cyanide releases 97% of the radiolabel while reduction of formate-labeled enzyme with NADH+ruthenium releases 80-85% of the radioactivity. These data are most simply interpreted by assuming that formate binds to the heme iron of cytochrome a3.

Animals↗

PubMed1996

A flash-photolysis study of the reactions of a caa3-type cytochrome oxidase with dioxygen and carbon monoxide.

The time course of absorbance changes following flash photolysis of the fully-reduced carboxycytochrome oxidase from Bacillus PS3 in the presence of O2 has been followed at 445, 550, 605, and 830 nm, and the results have been compared with the corresponding changes in bovine cytochrome oxidase. The PS3 enzyme has a covalently bound cytochrome c subunit and the fully-reduced species therefore accommodates five electrons instead of four as in the bovine enzyme. In the bovine enzyme, following CO dissociation, four phases were observed with time constants of about 10 microseconds, 30 microseconds, 100 microseconds, and I ms at 445 nm. The initial, 10-microsecond absorbance change at 445 nm is similar in the two enzymes. The subsequent phases involving heme a and CuA are not seen in the PS3 enzyme at 445 nm, because these redox centers are re-reduced by the covalently bound cytochrome c, as indicated by absorbance changes at 550 nm. A reaction scheme consistent with the experimental observations is presented. In addition, internal electron-transfer reactions in the absence of O2 were studied following flash-induced CO dissociation from the mixed-valence enzyme. Comparisons of the CO recombination rates in the mixed-valence and fully-reduced oxidases indicate that more electrons were transferred from heme a3 to a in PS3 oxidase compared to the bovine enzyme.

Animals↗

PubMed1999

Relationships between cytochrome oxidase (CO) blobs in primate primary visual cortex (V1) and the distribution of neurons projecting to the middle temporal area (MT).

The cytochrome oxidase (CO) blobs and interblobs in layer 3B of primate visual cortex have different sets of corticocortical connections. Cortical layers below layer 3B also project corticocortically, but the relationship of efferent projections from the deeper layers to the overlying blob/interblob architecture is less clear. We studied the tangential organization of neurons projecting from primary visual cortex (V1) to the middle temporal visual area (MT) and their relationship to the CO blobs. MT-projecting neurons in two primate species, bush babies and owl monkeys, were retrogradely labeled, then charted in tangential sections, and compared to the positions of the overlying CO blobs. In both primate species, MT-projecting neurons in layer 3C were unevenly distributed in the tangential plane, with dense patches of labeled cells that were aligned with the CO blobs. A novel two-dimensional spatial correlation method was used to show the colocalization of MT-projecting cells with the overlying blobs. Chi-square analyses performed with the cortical surface equally divided into compartments of blob, interblob, and blob/interblob borders showed that blob columns tended to have about 1.5 times more MT-projecting cells (P < 0.0001) than interblob columns. Similar analyses were applied to published data on V1 cells projecting to area MT in macaque monkey (Shipp and Zeki [1989] Euro J Neurosci 1:310-332). Again, the results showed a significant correlation between the cell distribution and CO blobs. Taken together, these results suggest that layer 3C is not uniform but is made up of a mosaic of cells that project to area MT and cells that project to some other location. These findings also indicate that the mosaic organization of layer 3C is related in some unique way to the overlying CO architecture.

Animals↗

PubMed1989

Superoxide dismutase and cytochrome oxidase activities in light and heavy synaptic mitochondria from rat cerebral cortex during aging.

The specific activities of superoxide dismutase (SOD) and cytochrome oxidase (COX) in light and heavy synaptic mitochondria from rat cerebral cortex at different ages (4, 8, 12, 16, 20, and 24 months) have been measured. The specific activity of COX was significantly higher in light synaptic mitochondria than in heavy ones at all ages examined. However, no significant difference during aging was shown. A marked decrease of SOD in light and heavy synaptic mitochondria during aging was observed.

Aging↗

PubMedDate not supplied

Nucleotide sequence of the cytochrome oxidase subunit 2 and val-tRNA genes and surrounding sequences from Kluyveromyces lactis K8 mitochondrial DNA.

The nucleotide sequence of the cytochrome oxidase subunit 2 (cox2) and val-tRNA genes and surrounding regions from Kluyveromyces lactis mitochondrial DNA is reported. Analysis of the coding region shows that the codons CUN (Thr), CGN (Arg) and AUA (Met) are absent in this gene. A single sequence, ATATAAGTAA, identical to the baker's yeast mtRNA polymerase recognition site, was detected upstream of val-tRNA. This sequence is absent from regions between val-tRNA-cox2 and cox2-cox1. In addition a sequence AATAATATTCTT, identical to the mRNA processing site in other yeast mitochondrial genomes is present 32-43 bp downstream to the TAA stop codon for the cox2 gene. Another short conserved sequence of 5 bp, TCTAA, is present upstream of the coding regions of cox2 genes in several yeasts, including K. lactis, but is not present upstream of other genes. Comparison of cox2 sequences from other organisms indicates that the mitochondrial DNA of K. lactis is closely related to that of Saccharomyces cerevisiae.

Amino Acid Sequence↗

PubMed1990

Cytochrome oxidase subunit II mRNAs in Oenothera mitochondria are edited at 24 sites.

Analysis of cDNA clones covering the entire coding region of cytochrome oxidase subunit II in Oenothera mitochondria reveals 24 potential editing sites: 23 C to U transitions and one U to C conversion. One editing event is observed outside the open reading frame in the 3' non-coding region. Thirteen editing sites are found altered in all cDNA clones, whereas the other eleven sites are only edited in some of the cDNA clones. These differentially edited sites occur most frequently at silent codon positions or in triplets at non-conserved amino acids.

Amino Acid Sequence↗

PubMed1983

Metabolic alterations in the hypothalamus of the Brattleboro rat demonstrated with cytochrome oxidase histochemistry.

Metabolic activity in the hypothalamus of homozygous and heterozygous Brattleboro rats and Long-Evans control rats was studied using cytochrome oxidase histochemistry. Increased metabolic activity was observed in the paraventricular nucleus (PVH), supraoptic nucleus (SON) and nucleus circularis (NC) of homozygous Brattleboro rats, and in the PVH of heterozygous rats. These results suggest that the metabolic activity of PVH and SON neurons is altered because of the inability of magnocellular neurosecretory neurons to produce vasopressin. In addition, the hyperactivity of neurons in the NC is probably related to the chronic dehydration present in these animals.

Animals↗

PubMed1978

The mechanism of reaction of fully reduced membrane-bound cytochrome oxidase with oxygen at 176K.

1. The results of non-linear optimization studies on the mechanism of reaction of fully reduced cytochrome oxidase with O2 at 176K are presented. The analysis is carried out on data obtained by means of dual-wavelength multi-channel spectroscopy at three wavelength pairs (604-630, 608-630 and 830-940 nm) and at three O2 concentrations (60, 200 and 1180 micron). The only model that satisfies the triple requirement of a standard deviation within the standard error of the experimental data, good determination of the optimized parameters and a random distribution of residuals is a three-species sequential mechanism. 2. On the basis of the optimized values of the relative absorption coefficients of the intermediates at each wavelength obtained from the present paper together with data from low-temperature trapping, e.p.r. and magnetic-susceptibility studies, the possible valence states of the metal centres in each of the intermediates are discussed.

Chemical Phenomena↗

PubMed1997

Regulation of murine cytochrome oxidase Vb gene expression in different tissues and during myogenesis. Role of a YY-1 factor-binding negative enhancer.

The mouse cytochrome oxidase (COX) Vb promoter contains three sequence motifs with partial or full consensus for YY-1 and GTG factor binding and a CArG box, located between positions -480 and -390. Individually, all three motifs stimulated transcription of the TKCAT promoter, and bound distinctly different proteins from the liver and differentiated C2C12 nuclear extracts. Collectively, these motifs, together with the downstream flanking sequence, -378 to -320, suppressed the transcription activity of heterologous promoters, thymidine kinase-chloramphenicol acetyltransferase (TKCAT) and COXIV/CAT. The transcription activities of both TKCAT and COXIV/CAT constructs were induced 3-4-fold during induced myogenesis of C2C12 cells. The downstream CArG-like motif binds transcription factor YY-1, while the upstream YY-1-like motif binds to a yet unidentified factor. Co-expression with intact YY-1, but not that lacking the DNA binding domain suppressed the transcriptional activity. Mutations targeted to the CArG-like motif abolished the suppressive effect of the negative enhancer and the inducibility of the promoter during myogenic differentiation. Our results suggest that the activity of the negative enhancer may determine the level of expression of the COX Vb gene in different tissues.

Animals↗

PubMed1985

Pea cytochrome oxidase subunit II gene has no intron and generates two mRNA transcripts with different 5'-termini.

We have isolated and sequenced the cytochrome oxidase subunit II (COII) gene from pea mitochondria. The coding sequence (777 bp) shows over 90% homology to the COII genes from three monocotyledonous plants (rice, maize and wheat) and one dicotyledonous plant (Oenothera berteriana). Several codons are deleted, however, in the pea COII gene. Of interest is the deletion in pea of the last three codons, including the stop codon, found at the 3' end of the other four COII genes. Instead, a new stop codon has been created due to a single-base substitution at the 13th bp downstream from the position of the original stop codon. This pea gene does not contain an intron which is found in all three monocots. Two distinct 5' termini of the pea COII transcripts have been identified by S1 nuclease mapping, one at 285 bp (site I) and the other at 302 bp (site II) upstream from the ATG codon. They are located at two identical sites within nearly perfect direct repeats. Transcripts with the 5' end corresponding to site I occur five time more frequently than those with the 5' end corresponding to site II. Both transcripts have the same 3' terminus which has been mapped to be at 193 to 195 bp downstream from the stop codon.

Base Sequence↗

PubMed1992

Cytochrome oxidase as a redox-linked proton pump.

Some general principles for redox-linked proton pumps are described and applied to cytochrome oxidase. A reaction scheme obeying these principles is described. The scheme includes electron transfer between the redox centers of the oxidase, the mechanism of dioxygen reduction, protonation and deprotonation steps for both scalar and vectorial protons, as well as input-output transitions for electrons and protons. It is consistent with a large amount of kinetic information.

Electron Transport↗

PubMed1991

[Spatial organization of cytochrome oxidase subunit II].

We have studied the tryptic digestion and cyanogen bromide cleavage of the tritium-labelled subunit II from bovine cytochrome oxidase. Basing on the radioactivity distribution in the peptides obtained we suggest a model for the spatial structure of the title subunit.

Amino Acid Sequence↗

PubMed1987

Connections between layer 4B of area 17 and the thick cytochrome oxidase stripes of area 18 in the squirrel monkey.

In area 18 of the primate visual cortex, staining for the mitochondrial enzyme cytochrome oxidase reveals 3 types of stripelike subdivisions running perpendicular to the 17/18 border: thick, thin, and pale stripes. In a previous paper (Livingstone and Hubel, 1984), we described the anatomical connections with area 17 of 2 of these 3 subdivisions, but we did not have any conclusive information on the third subdivision, the thick stripes. Here we report that, in the squirrel monkey, the main input to the thick stripes from area 17 arises from layer 4B. Layer 4B receives its input from the magnocellular division of the lateral geniculate body by way of layer 4C alpha; the thick stripes therefore probably belong to the magnocellular subdivision of the visual pathway.

Animals↗

PubMed1993

A survey of auditory brainstem nuclei in the chicken (Gallus domesticus) with cytochrome oxidase histochemistry.

The chicken's auditory brainstem nuclei from the cochlear nuclei to the nuclei of the lateral leminiscus were studied with cytochrome oxidase histochemistry. A strong reactivity in the cochlear and laminar nuclei was confirmed. Additional structures displaying high activity levels include the superior olive and both partitions of the nucleus intermedius lemnisci lateralis. Unilateral cochlea removal led to a strong reduction of activity in the cochlear nuclei and the nucleus laminaris, whereas there was no remarkable effect in higher brainstem centers. After bilateral cochlea extirpation auditory structures still displayed higher enzyme levels than most other nuclei. These observations point to the extraordinary metabolic activity in the ascending auditory pathway which is largely independent of sensory input from the auditory nerve.

Animals↗