• 제목/요약/키워드: cytochrome oxidase

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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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    • 제44권3호
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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.

둥근마(Dioscorea bulbifera)를 가해하는 뿌리혹선충(Meloidogyne sp. HSC)의 Cytochrome Oxidase Subunit II (COII) 염기서열 분석 (Cytochrome Oxidase Subunit II (COII) Sequence Analysis of Root-knot Nematode, Meloidogyne sp. HSC, Infesting Yam (Dioscorea bulbifera))

  • 한상찬;강상진;김용균
    • 한국응용곤충학회지
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    • 제46권1호
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    • pp.169-173
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    • 2007
  • 경북 안동에서 재배하는 둥근마(Dioscorea bulbifera)에서 뿌리혹선충 피해가 발견되었다. 피해 괴경에서 다수의 암컷 선충을 분리하였고, 이들의 cytochrome oxidase subunit II (COII) DNA 서열을 분석하였다. 둥근마의 뿌리혹 형성을 유도하는 식물 선충의 COII 유전자위 크기와 염기서열은 Meloidogyne javanica 또는 M. incognita의 해당 영역과 높은 유사도를 보였다. 그러나 이들 두 종을 구분하는데 이용되는 제한효소(HinfI)위치에 있어서 본 둥근마로부터 분리된 뿌리혹선충은 이들 두 종과 뚜렷한 차이를 보였다.

Changes in Cytochrome c Oxidase and NO in Rat Lung Mitochondria Following Iron Overload

  • Kim, Min-Sun;Hong, Min-A;Song, Eun-Sook
    • Animal cells and systems
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    • 제13권2호
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    • pp.105-112
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    • 2009
  • In this study, the effects of iron on cytochrome c oxidase (CcO) in rat lung mitochondria were examined. Similar to liver mitochondria, iron accumulated considerably in lung mitochondria (more than 2-fold). Likewise, the reactive oxygen species and nitric oxide (NO) content of mitochondria were increased by more than 50% and 100%, respectively. NO might be produced by nitric oxide synthase (NOS), eNOS and iNOS type, with particular contribution by NOS in mitochondria. The respiratory control ratio of iron overloaded lung mitochondria dropped to nearly 50% due to increased state 4. Likewise, cytochrome c oxidase activity was lowered significantly to approximately 50% due to excess iron. Real-time PCR revealed that the expression of isoforms 1 and 2 of subunit IV of CeO was enhanced greatly under excess iron conditions. Taken together, these results show that oxidative phosphorylation within lung mitochondria may be influenced by iron overload through changes in cytochrome c oxidase and NO.

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
    • 통합자연과학논문집
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    • 제15권2호
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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.

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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    • 제28권4호
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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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쥐 근조직의 Cytochrome Oxidase에 대한 비교 연구 (Comparative Study on Cytochrome Oxidase of Rat Muscle Tissues)

  • Song, Eun-Sook
    • 한국동물학회지
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    • 제29권1호
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    • pp.70-74
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    • 1986
  • 쥐 골격근의 크루드 미토콘드리아에 있는 시토크롬 옥시다제의 활성을 비교 하였다. 붉은색의 빠른 트윗치 근육은 가장 높은 효소 활성을 나타냈고, 흰색의 빠른 트읫치 근육은 가장 낮았으며, 붉은 색이며 느린 트윗치 근육은 그 중간이었다. 위 세가지 타입의 근육에서 힘 염색한 결과 시토크롬 옥시다제의 전기영동상의 이동성이 다르게 나타났다. 이동성의 순서는 타입 I > 타입 $II_A$ > 타입 $II_B$이었다. 면역학적 전기영동의 결과는 위의 결과를 뒷받침 하였다.

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

  • 김진상
    • 대한수의학회지
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    • 제29권4호
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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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Rhodobacter sphaeroides 2.4.1 내의 pyridine nucleotide와 quinone pool의 redox 상태와 광합성기구의 합성과의 상관관계 (Relationship of the Redox State of Pyridine Nucleotides and Quinone Pool with Spectral Complex Formation in Rhodobacter sphaeroides 2.4.1)

  • 고인정;오정일
    • 생명과학회지
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    • 제19권7호
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    • pp.852-858
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    • 2009
  • 호흡전자전달계의 cytochrome bc$_1$ complex 또는 cytochrome c oxidase가 기능을 하지 않는 Rhodobacter sphaeroides mutant 내에서 pyridine nucleotide[NAD(P)H와 NAD(P)$^+$]의 농도와 redox 상태는 wild type과 비교할 때 큰 변화가 없었다. 높은 산소분압 조건에서 키운 Rhodobacter sphaeroides cbb$_3$ oxidase mutant 내에서 PrrBA two-component system에 의해서 조절되는 puf 오페론의 발현은 pyridine nucleotide나 전자전달계의 ubiquinone/ubiquinol pool의 redox 상태의 변화에 의해 유도된 것이 아니다. R. sphaeroides cytochrome bc$_1$ complex mutant를 이용하여 광합성기구 합성에 대한 cbb$_3$ cytochrome c oxidase의 억제 효과는 ubiquinone/ubiquinol pool의 redox 변화에 의해 간접적으로 일어나는 것이 아님을 증명하였다.

DIFFERENTIAL INDUCTION OF RAT LIVER MICROSOMAL CYTOCHROME-DEPENDENT MONOOXYGENASE AND UDP-GLUCURONOSYLTRANSFERASE ACTIVITIES BY VARIOUS NARCOTIC DRUGS

  • Hong, Young-Sook;Pae, Young-Sook
    • Toxicological Research
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    • 제5권1호
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    • pp.17-25
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    • 1989
  • Chronic adminstraction of morphine to adult male rats has long been known to lower hepatic cytochrome p-450 content and its dependent mixed-function oxidase activity. Following the treatment of adult male rats with morphine, pethidine pentazocine and codeine and also by concomitant adminstration of naloxone activities of microsomal electron transfer in the adult male rats were examined. In present study, the acute treatment of mature male rats with a dose of narcotic drugs higher than that used chronically also reduces their hepatic cytochrome p-450.

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