Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.9.3.1 (cytochrome oxidase)
8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The complete amino acid sequence of the heme alpha-containing subunit V of bovine heart cytochrome oxidase was determined to be: H2N-Ser-His-Gly-Ser-His-Glu-Thr-Asp-Glu-Glu-Phe-Asp-Ala-Arg-Trp-Val-Thr-Tyr-Phe-Asn-Lys-Pro-Asp-Ile-Asp-Ala-Trp-Glu-Leu-Arg-Lys-Gly-Met-Asn-Thr-Leu-Val-Gly-Tyr-Asp-Leu-Val-Pro-Glu-Pro-Lys-Ile-Ile-Asp-Ala-Ala-Leu-Arg-Ala-Cys-Arg-Arg-Leu-Asn-Asp-Phe-Ala-Ser-Ala-Val-Arg-Ile-Leu-Glu-Val-Val-Lys-Asp-Lys-Ala-Gly-Pro-His-Lys-Glu-Ile-Tyr-Pro-Tyr-Val-Ile-Gln-Glu-Leu-Arg-Pro-Thr-Leu-Asn-Glu-Leu-Gly-Ile-Ser-Thr-Pro-Glu-Glu-Leu-Gly-Leu-Asp-Lys-Val-COOH. The subunit V is a single polypeptide which consists of 109 amino acid residues. The protein contains 48.6% hydrophobic residues and 34.0% hydrophilic residues and it is an acidic protein having a net charge of -3 at neutral pH. The molecular weight of subunit V was calculated to be 12,436 and that for the heme alpha-containing polypeptide was 13,295.
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PMID:Amino acid sequence of subunit V of bovine heart cytochrome oxidase, the heme alpha-containing subunit. 22 Feb 24

The gene (coxII) encoding subunit II of Rhodobacter sphaeroides cytochrome c oxidase (cytochrome aa3) has been isolated by screening a genomic DNA library in phage lambda with a probe derived from coxII of Paracoccus denitrificans. A 2-kb fragment containing coxII DNA was subcloned into the phage M13mp18 and the sequence determined. The 2-kb insert contains the entire coding region for coxII gene, including the ATG start codon and a TGA stop codon. The deduced amino acid (aa) sequence of subunit II of R. sphaeroides shows regions of substantial homology to the corresponding subunit of the bovine mitochondrial oxidase (63% overall) and P. denitrificans oxidase (68% overall). The postulated redox-active copper ion (CuA) binding site involving two Cys and two His residues (as well as an alternative Met residue) is conserved among these species, along with four invariant acidic aa residues (two Asp and two Glu) that may be involved in interactions with cytochrome c, and a region of aromatic residues (Tyr-Gln-Trp-Tyr-Trp-Gly-Tyr-Glu-Tyr) which is postulated to play a role in electron transfer. Hydropathy profile analysis suggests that while the bovine COXII secondary structure contains two transmembrane helices, the R. sphaeroides subunit II has a third such helix that may function as part of a signal sequence, as suggested for P. denitrificans.
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PMID:The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides; comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species. 164 8

The neuronal uptake and laminar distribution of cortically injected tritium-labeled gamma-aminobutyrate (GABA), aspartic acid, glutamate and glycine was examined in the prestriate cortex of squirrel monkeys. The intent of this investigation was not to examine the role of these amino acids as neurotransmitters, but to correlate the distribution of tritium-labeled neurons with their levels of cytochrome oxidase activity. A comparison of the number of these labeled neurons was made between the metabolically active "puff" and the less active "nonpuff" regions. In addition, these results were contrasted with the findings in area 17. With each tritiated amino acid tested, labeled neurons that had either high or low levels of cytochrome oxidase activity were present in all laminae. However, the density of labeled neurons varied between lamina for a given amino acid as well as between different amino acids. While many neurons that were cytochrome oxidase-reactive were also tritium-labeled, cytochrome oxidase activity was not a prerequisite for the sequestering of tritium label. In fact, many of the labeled neurons exhibited relatively low levels of cytochrome oxidase activity. Similar to area 17, few aspartate- or glutamate-labeled neurons were present in laminae II-III. The number of labeled neurons for both amino acids increased in laminae IV-VI, with the greatest increase observed in laminae V-VI. Gamma-aminobutyrate-labeled neurons were more prevalent in laminae I and upper II than in the other laminae, whereas in area 17, a greater proportion of the labeled neurons were found in laminae V-VI. With the exception of the uppermost laminae, where GABA-labeled neurons were more abundant, the number of glycine-labeled neurons was significantly greater throughout most laminae than with the other amino acids examined. The density of glycine-labeled neurons in lamina IV, however, was significantly less than the number observed in lamina III even though lamina III was farther away from the injection site which was at the boundary between laminae V-VI. Glycine-labeled neurons were, on average, larger than those labeled with any other amino acid. Similar to area 17, more GABA- and glycine-labeled neurons were observed within the puff regions than in nonpuff regions. No puff/nonpuff differences were observed in the distribution of leucine-injected controls. Labeled neurons for each amino acid included stellate-, fusiform- and pyramidal-shaped cells, each of varying sizes. However, outside the intensely labeled injection sites, no GABA-labeled pyramidal cells were observed.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Neuronal uptake and laminar distribution of tritiated aspartate, glutamate, gamma-aminobutyrate and glycine in the prestriate cortex of squirrel monkeys: correlation with levels of cytochrome oxidase activity and their uptake in area 17. 289 Jan 20

The proteolytic processing of the mitochondrially encoded subunit II of cytochrome oxidase is prevented by the yeast mutation ts2858. We report that the mutant is, in addition, temperature sensitive for the processing of cytochrome b2, a protein encoded by nuclear DNA. Thus the same mutation affects the removal of pre-sequences from a mitochondrially encoded inner membrane protein and from an imported soluble protein located in the intermembrane space. The mutation blocks the second processing step of cytochrome b2. The cytochrome b2 intermediate accumulates in the mutant at 36 degrees C and assumes its enzyme activity. At 23 degrees C the conversion to the mature protein is considerably slower than in wild-type cells. The similarity of the cleavage sites Asn-Asp and Asn-Glu of the precursors for cytochrome oxidase subunit II and cytochrome b2, respectively, suggests a sequence-specific recognition by one protease or a factor activating a protease. On the other hand maturation of cytochrome c peroxidase, another enzyme of the intermembrane space, is not affected by the pet ts2858 mutation.
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PMID:One nuclear gene controls the removal of transient pre-sequences from two yeast proteins: one encoded by the nuclear the other by the mitochondrial genome. 301 96

Substoichiometric amounts of Mn are bound by the aa3-type cytochrome c oxidase of Rhodobacter sphaeroides and appear in the EPR spectrum of the purified enzyme as signals that overlay those of CuA in the g = 2.0 region. The Mn is tightly bound and not removed by a high degree of purification or by washing with 50 mM EDTA. The amount of bound Mn varies with the ratio of Mg to Mn in the growth medium. Oxidase containing no EPR-detectable Mn can be prepared from cells grown in low Mn/Mg, while high Mn/Mg in the growth medium gives rise to near stoichiometric levels (0.7 mol/mol of aa3). Incubation of purified Mn-deficient oxidase with 1 mM Mn does not allow incorporation into the tight binding site, indicating that this site is not accessible in the assembled protein. When bound Mn is depleted by growth in high Mg, there is no change in electron transfer activity, suggesting that Mg may substituted for Mn and maintain protein structure. Analysis of site-directed mutants in an extramembrane loop close to the active site of cytochrome oxidase identifies His-411 and Asp-412 of subunit I as probable ligands of the Mn. Mutation of either residue leads to lower activity and loss of Mn binding, even in cells grown in elevated concentrations of Mn. Since Mn binding correlates with the [Mn] to [Mg] ratio in the culture medium, we propose that Mn competes for the site that normally binds a stoichiometric Mg ion in aa3-type cytochrome c oxidases.
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PMID:Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides. 777 4

The cyt-12-12 mutant of Neurospora crassa is characterized by slow growth and a deficiency of spectrophotometrically-detectable cytochromes aa3 and c. Using a sib-selection procedure we have isolated the cyt-12+ allele from a cosmid library of N. crassa genomic DNA. Characterization of the cyt-12+ allele reveals that it encodes the structural gene for cytochrome c. DNA sequence analysis of the cyt-12-12 allele revealed a mutation in the cytochrome c coding sequence that results in replacement of a glycine residue, which is invariant in the cytochrome c of other species, with an aspartic acid. Genetic analysis confirms that cyt-12-12 is allelic with the previously-characterized cyc-1-1 mutant, which was also shown to affect the single locus encoding cytochrome c in N. crassa. We suggest that the amount of functional cytochrome c present in mitochondria influences the level of cytochrome aa3.
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PMID:Mutations in the structural gene for cytochrome c result in deficiency of both cytochromes aa3 and c in Neurospora crassa. 788 27

Progressive exercise intolerance was associated with a decreased maximal rate of ubiquinol cytochrome c reductase (complex III) activity in the muscle mitochondria of the studied patient and with a thirty five-fold increase in the I50 for antimycin A. In contrast, myxothiazol sensitivity was not altered. Complex III activity was stable at 37 degrees C, but progressively decreased at 4 degrees C. An heteroplasmic G to A mutation at position 15615 of the mitochondrial DNA, resulting in the replacement of the highly conserved Gly290 in cytochrome b by Asp, was identified. Histochemical studies showed increased cytochrome oxidase and succinate dehydrogenase activities under the sarcolemma of type I fibres. After partial extraction of mitochondria from the muscle, the residual pellet contained a lower percentage of the mutation than did whole muscle, suggesting that the percentage of mutation is higher in the most readily extracted mitochondria, most probably present under the sarcolemma. In the current 8 transmembrane helix model of cytochrome b, Gly290 lies at the end of the sixth transmembrane helix, facing the intermembrane space and close to the presumed sites of interaction between cytochrome b, the iron-sulfur protein and the 9.5 kDa protein. Since immunoblotting experiments showed a relative decrease in the proportions of these three subunits in the patient's mitochondria compared with the other complex III subunits, it is probable that the complex III instability and the relative decrease in these subunits are related to the mutation. The relationship between the decrease in the apparent affinity for antimycin A and the instability of complex III are discussed.
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PMID:Antimycin resistance and ubiquinol cytochrome c reductase instability associated with a human cytochrome b mutation. 898 36

Probes were cloned, characterized, and developed for all regions of the mitochondrial DNA (mtDNA) of pejerrey Odontesthes bonariensis to provide the basis for the study of genetic diversity of South American atherinopsinii and to enable species identification from small amounts of tissue. The mtDNA was extracted from liver and cleaved with Eco RI, producing four fragments (7·4, 3·4, 3·1 and 2·9 kb) which were cloned using pUC118 plasmid vectors. Sequence analysis from both ends of the fragments showed that they encode tRNA (Asp, Phe, and Ser-TGA), 12 S rRNA, cytochrome oxidase (CO) II, NADH 4, 5, and 6, and the d-loop, and that the relative positions of these genes are identical to those in the mtDNA of other teleosts. A comparison of homology with carp mtDNA nucleotide sequences revealed that tRNA (Phe and Ser-TGA) and CO II were relatively conserved, whereas the d-loop region was highly divergent. The cloned mtDNA probes detected mtDNA fragments from about 800 ng of total DNA extracted from liver, muscle, and single embryos of O. bonariensis, and were effective for restriction length fragment polymorphism (RFLP) analysis of Patagonina hatcheri, the most distant atherinopsine relative of pejerrey. The cloned mtDNA probes may be useful for the analysis of genetic diversity and non-destructive species identification, including the examin-ation of eggs, larvae and juveniles. The mtDNA sequences reported here provide the basis for the design of primers for PCR-based RFLP analysis. 1997 The Fisheries Society of the British Isles
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PMID:Cloning and characterization of pejerrey mitochondrial DNA and its application for RFLP analysis 923 99

Cytochrome c (cyt c) release was investigated in cerebellar granule cells used as an in vitro neuronal model of apoptosis. We have found that cyt c is released into the cytoplasm as an intact, functionally active protein, that this event occurs early, in the commitment phase of the apoptotic process, and that after accumulation, this protein is progressively degraded. Degradation, but not release, is fully blocked by benzyloxycarbonyl-Val-Ala-Asp-fluoromethylchetone (z-VAD-fmk). On the basis of previous findings obtained in the same neuronal population undergoing excitotoxic death, it is hypothesized that release of cyt c may be part of a cellular attempt to maintain production of ATP via cytochrome oxidase, which is reduced by cytosolic NADH in a cytochrome b5-soluble cyt c-mediated fashion.
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PMID:Early release and subsequent caspase-mediated degradation of cytochrome c in apoptotic cerebellar granule cells. 1048 78

Evidence is increasing that mitochondrial dysfunction is involved in amyotrophic lateral sclerosis, a neurodegenerative disease characterized by selective motoneuron death. To study the role of mitochondrial dysfunction in the pathways leading to motoneuron death, we developed an in vitro model of chronic motoneuron toxicity, based on malonate-induced inhibition of complex II in the mitochondrial electron transport chain. Treatment with malonate resulted in a dose-dependent decrease in cellular ATP levels. We observed that motoneurons were significantly more vulnerable to mitochondrial inhibition than control neurons in the dorsal horn. We could reproduce this dose-dependent phenomenon with the complex IV inhibitor sodium azide. The free radical scavenger alpha-phenyl-N-tert-butylnitrone, the AMPA/kainate receptor blocker 6-cyano-7-nitroquinoxaline-2,3-dione, and riluzole, a drug that is currently used for the treatment of amyotrophic lateral sclerosis, were protective against malonate-induced motoneuron death. Furthermore, the caspase inhibitors N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone and z-Asp-Glu-Val-Asp-fluoromethyl ketone were both protective against malonate toxicity. Our model shows that chronic mitochondrial inhibition leads to selective motoneuron death, which is most likely apoptotic.
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PMID:Chronic mitochondrial inhibition induces selective motoneuron death in vitro: a new model for amyotrophic lateral sclerosis. 1069 48


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