• Title/Summary/Keyword: cytochrome c oxidase

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Inhibitory Effects of Exogenous Cu2+ and Zn2+ on the Cytochrome c Oxidase Activity

  • Min, Tong-Pil;Han, Sang-Hwa
    • BMB Reports
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    • v.28 no.4
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    • pp.311-315
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    • 1995
  • Exogenous $Cu^{2+}$ or $Zn^{2+}$ at micromolar concentration had a strong inhibitory effect on detergent-solubilized cytochrome c oxidase. A similar effect was observed when $Cu^{2+}$ was added to vesicular cytochrome c oxidase, although the extent of inhibition was significantly larger for the uncoupled state than for the coupled state. Interestingly, the inhibition by $Zn^{2+}$ was almost negligible for both the coupled and uncoupled states. These results suggest that the binding sites for $Cu^{2+}$ ions are exposed to the extravesicular side. whereas those for $Zn^{2+}$ are exposed to the matrix side. The EPR spectra of bound $Cu^{2+}$ ions at 77 K indicate that each of the first two $Cu^{2+}$ ions is ligated by three or four histidine residues, as evidenced by distinct $^{14}N$ superhyperfine splitting. These $Cu^{2+}$ ions can not be removed readily by EDTA and inhibit the enzyme activity by as much as 80%.

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Effect of Mutations of Five Conserved Histidine Residues in the Catalytic Subunit of the cbb3 Cytochrome c Oxidase on its Function

  • Oh Jeong-Il
    • Journal of Microbiology
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    • v.44 no.3
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    • pp.284-292
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    • 2006
  • The cbb3 cytochrome c oxidase has the dual function as a terminal oxidase and oxygen sensor in the photosynthetic bacterium, Rhodobacter sphaeroides. The cbb3 oxidase forms a signal transduction pathway together with the PrrBA two-component system that controls photosynthesis gene expression in response to changes in oxygen tension in the environment. Under aerobic conditions the cbb3 oxidase generates an inhibitory signal, which shifts the equilibrium of PrrB kinase/phosphatase activities towards the phosphatase mode. Photosynthesis genes are thereby turned off under aerobic conditions. The catalytic subunit (CcoN) of the R. sphaeroides cbb3 oxidase contains five histidine residues (H2l4, B233, H303, H320, and H444) that are conserved in all CcoN subunits of the cbb3 oxidase, but not in the catalytic subunits of other members of copper-heme superfamily oxidases. H214A mutation of CcoN affected neither catalytic activity nor sensory (signaling) function of the cbb3 oxidase, whereas H320A mutation led to almost complete loss of both catalytic activity and sensory function of the cbb3 oxidase. H233V and H444A mutations brought about the partial loss of catalytic activity and sensory function of the cbb3 oxidase. Interestingly, the H303A mutant form of the cbb3 oxidase retains the catalytic function as a cytochrome c oxidase as compared to the wild-type oxidase, while it is defective in signaling function as an oxygen sensor. H303 appears to be implicated in either signal sensing or generation of the inhibitory signal to the PrrBA two-component system.

Relationship of the Redox State of Pyridine Nucleotides and Quinone Pool with Spectral Complex Formation in Rhodobacter sphaeroides 2.4.1 (Rhodobacter sphaeroides 2.4.1 내의 pyridine nucleotide와 quinone pool의 redox 상태와 광합성기구의 합성과의 상관관계)

  • Ko, In-Jeong;Oh, Jeong-Il
    • Journal of Life Science
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    • v.19 no.7
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    • pp.852-858
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    • 2009
  • The homeostasis of the pyridine nucleotide pool [NAD(P)H and NAD(P)$^+$] is maintained in Rhodobacter sphaeroides mutant strains defective in the cytochrome bci complex or the cytochrome c oxidases in terms of its concentration and redox state. Aerobic derepression of the puf operon, which is under the control of the PrrBA two-component system, in the CBB3 mutant strain of R. sphaeroides was shown to be not the result of changes in the redox state of the pyridine nucleotides and the ubiquinone/ubiquinol pool. Using the bc$_1$ complex knock-out mutant strain of R. sphaeroides, we clearly demonstrated that the inhibitory effect of cbb$_3$, oxidase on spectral complex formation is not caused indirectly by the redox change of the ubiquinone/ubiquinol pool.

Distribution of Calretinin and Calbindin-immnorectivity in Subregions with the Low Cytochrome Oxidase Reacitivity in the Periaquedectal Gray of Rats

  • Park, Sah-Hoon;Kim, Kun-Hee;Park, Jong-Seong
    • Journal of Integrative Natural Science
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    • v.15 no.2
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    • pp.63-72
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    • 2022
  • To elucidate the neurochemical characteristics of the midbrain periaqueductal gray (PAG), the distribution patterns of several neuroanatomical markers within the PAG were compared. Immunohistochemical staining for the intracellular calcium binding proteins including calbindin, calretinin, and parvalbumin and histochemical staining for cytochrome oxidase, acetylcholinesterase, and NADPH-diaphorase were performed in. Each chemical substance were localized in the specific subregions within PAG. Calbindin- immunoreactivity were selectively distributed in the dorsolateral PAG, the ventral half of lateral PAG, the ventralateral PAG, and supraoculomotor cap (Su3C) nucleus. Distribution of calretinin-immunoreactivity were generally similar with that of clabindin, but showed relatively low subregional selectivity. Parvalbumin-immunoreactivity was very poor within the PAG. High reactivity of cytochrome oxidase were found in the dorsomedial PAG and the lateral half of lateral PAG, in which calbindin- and calretinin-immunoreactive perikarya were scarcely observed. Acetylcholinesterase distribution was similar with that of cytochrome oxidase, and the difference was in the additional marking of of Su3C with acetylcholinesterase. Results of the present study provides data for the further subdivisions of the territory of the PAG compared to the presently accepted subregions within the PAG.

Purification of Cytochrome c-551 from Photosynthetic Bacterium Rhodopseudomonas Gelatinosa ATCC 17013 (광합성 세균인 Rhodopseudomonas gelatinosa ATCC 17013에서 Cytochrome c-551의 정체)

  • 강대길;최원기
    • Korean Journal of Microbiology
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    • v.29 no.2
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    • pp.92-96
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    • 1991
  • The soluble cytochrome c-551 of photosynthetic bacterium, Rhodopseudomonas gelatinosa ATCC 17013 was purified through a sequene of four step chromatography including CM-cellulose ion-exchange chromatography, DEAE-Sephacel chromatography, Sephacryl s-200 gel permeation chromatography, and HPLC (SP-5PW). The molecular weight of the purified cytochrome c-551 was 14, 600 Da, and this protein shows the absorption peak at 551 nm, 522 nm, and 417 nm as the reduced form, and at 412 nm as the oxidized form. The cytochrome c-551 seems to be a substrate for the terminal oxidase in the electron transport chain.

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Histochemical studies on effect of low concentrated carbon monoxide on the caudate nucleus in rat (저농도 일산화탄소가 흰쥐 미상핵에 미치는 영향에 관한 조직화학적 연구)

  • Kim, Jin-sang
    • Korean Journal of Veterinary Research
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    • v.29 no.4
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    • pp.425-431
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    • 1989
  • This study was undertaken to investigate the changes of enzyme activities resulted from low concentrated carbon monoxide poisoning on the caudate nucleus in rat. The activities of cytochrome oxidase, succinate dehydrogenase and lactate dehydragenase were observed histochemically, after the experimental animals were poisoned to 100ppm carbon monoxide for 8 hours every day from one day to 16 days. The materials were sliced from coronal section at the level of the optic chiasm and immediately frozen sections of $10{\mu}m$ thickness were cut on the cryostat at $-15^{\circ}C$ and incubated in the medium containing substrate for histochemical detection of cytochrome oxidase, succinate dehydrogenase and lactate dehydrogenase. The sections were mounted in glycerol gelatin and observed under light microscope. It was obtained that cytochrome oxidase activity decreased moderately and succinate dehydrogenase activity showed marked or moderate activity during entire poisoning period and lactate dehydrogenase activity showed marked or moderate activity from one to 8 days but recovered to normal condition at 16th day.

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Phylogenetic Analysis of Reticulitermes speratus using the Mitochondrial Cytochrome C Oxidase Subunit I Gene

  • Cho, Moon-Jung;Shin, Keum;Kim, Young-Kyoon;Kim, Yeong-Suk;Kim, Tae-Jong
    • Journal of the Korean Wood Science and Technology
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    • v.38 no.2
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    • pp.135-139
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    • 2010
  • Reticulitermes speratus is commonly found in Asia, including Korea and Japan. We recently analyzed the 5' region of mitochondrial cytochrome c oxidase subunit I to perform a phylogenetic analysis of R. speratus KMT1, isolated in Seoul, Korea. Our results, using COXI, suggest that the taxonomy of R. speratus should be reconsidered with regard to the subgenus group. A similar phylogenetic analysis by COXI and COXII demonstrated the reliability of COXI genetic information in a molecular phylogenetic analysis of termites.

Stock Characterization of the Fleshy Prawn (Penaeus chinensis) in the Yellow Sea by Intraspecific Sequence Variation of the Cytochrome c Oxidase Subunit I Gene

  • HWANG Gyu-Lin
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.29 no.6
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    • pp.876-881
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    • 1996
  • To determine the amount of genetic variation among populations of Penaeus chinensis (Osbeck) in the Yellow Sea, 342 bp region of the mitochondrial cytochrome c oxidase subunit I gene was amplified and sequenced. Six haplotypes, which differ by from one to four nucleotide sustitutions, were detected from 34 individuals of 4 populations examined. Mean sequence divergence between pairs of haplotypes was $0.68\%$. Most individuals from 4 populations were shared by the most common genotype. This genotype was distributed evenly in the Korean and Chinese populations. This result is in accordance with findings observed using RFLPs analysis of mtDNA (Hwang et al., 1997). Therefore, it is suggested that P. chinensis should be treated as one unit stock in the Yellow Sea.

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The Effects of Acupuncture at LR3 Acupoint on Mitochondrial Complex IV Oxidase activity in Liver (태충 침자가 간 미토콘드리아 내 Complex IV에 미치는 영향)

  • Choi, Donghee;Lee, Yumi;Kim, Mirae;Park, Jeonghye;Kim, Hyeran;Na, Changsu;Youn, Daehwan
    • Korean Journal of Acupuncture
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    • v.36 no.4
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    • pp.200-209
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    • 2019
  • Objectives : The liver is rich in mitochondria and it plays a key role in whole-body energy homeostasis. Mitochondria is double membrane-bound organelle that supplies energy for intracellular metabolism including Krebs cycle and beta-oxidation. Acupuncture is known to stimulate and regulate the flow of energy. To explore the effect of acupuncture on the mitochondrial respiratory chain activity in the rats' livers, the activity of mitochondrial respiratory chain complexes I to IV was observed. Methods : The rats were divided into 4 groups; Normal 1 (no acupuncture treatment and anesthesia for 5 min), Normal 2 (no acupuncture treatment and anesthesia for 10 min), MA1 (acupuncture treatment at bilateral LR3 under anesthesia for 5 min), and MA2 (acupuncture treatment at bilateral LR3 under anesthesia for 10 min). All rats were sacrificed and the livers were examined for respiratory chain change. Results : There was no difference in ubiquinon oxidoreductase, succinate dehydrogenase, and ubiquinol cytochrome C oxidoreductase after acupuncture at LR3. Acupuncture at LR3 for 10 min increased the activity of cytochrome C oxidase compared with no acupuncture groups. Conclusions : Acupuncture at LR3 mediated mitochondrial respiratory chain activity via the cytochrome C oxidase signaling pathway in the livers of rats.

Effects of Local Anesthetics on Electron Transport and Generation of Superoxide Radicals in Mitochondria (국소마취제가 Mitochondria에서의 전자이동 및 Superoxide Radicals의 생성에 미치는 영향)

  • Lee, Chung-Soo;Shin, Yong-Kyoo;Lee, Kwang-Soo
    • The Korean Journal of Pharmacology
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    • v.23 no.2
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    • pp.113-121
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    • 1987
  • Local anesthetics were investigated for their effects on mitochondrial electron transport system, production of superoxide radical from submitochondrial particles and malondialdehyde production through lipid per oxidation. Local anesthetics had various effects on activities of enzymes in electron transport chain. The activities of NADH dehydrogenase, NADH oxidase and NADH-ubiquinone oxidoreductase were effectively inhibited by lidocaine, procaine and dibucaine but slightly influenced by cocaine. The activities of succinate dehydrogenase, succinate-cytochrome c oxidoreductase and succinate-ubiquinone oxidoreductase were inhibited by lidocaine and dibucaine, but the succinate oxidase activity was stimulated by local anesthetics. Both dihydroubiquinone-cytochrome c oxidoreductase and cytochrome c oxidase activities were inhibited by local anesthetics. In these reactions, the response of Complex I segment to local anesthetics was greater than other Complex segments. Local anesthetics inhibited both the superoxide production from submitochondrial particles supplemented with succinate or NADH and the enhanced production of superoxide radicals by antimycin. The malondialdehyde production by oxygen free radicals was inhibited by local anesthetics. These results suggest that the inhibition of superoxide and malondialdehyde production caused by local anesthetics may be brought by suppression of the electron transport in mitochondria at sites in or near complex I segment.

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