チトクロムb、シトクロムb
WordNet
- put to bed; "The children were bedded at ten oclock"
- a foundation of earth or rock supporting a road or railroad track; "the track bed had washed away"
- a piece of furniture that provides a place to sleep; "he sat on the edge of the bed"; "the room had only a bed and chair"
- a plot of ground in which plants are growing; "the gardener planted a bed of roses"
- the flat surface of a printing press on which the type form is laid in the last stage of producing a newspaper or magazine or book etc.
- a depression forming the ground under a body of water; "he searched for treasure on the ocean bed" (同)bottom
- (geology) a stratum of rock (especially sedimentary rock); "they found a bed of sandstone"
- furnish with a bed; "The inn keeper could bed all the new arrivals"
- place (plants) in a prepared bed of soil
- the 2nd letter of the Roman alphabet (同)b
- the blood group whose red cells carry the B antigen (同)type_B, group B
- (biochemistry) a class of hemoprotein whose principal biological function is electron transfer (especially in cellular respiration)
PrepTutorEJDIC
- 〈C〉〈U〉『ベット』,『寝台』 / 〈U〉睡眠,宿泊 / 〈C〉『花壇,苗床…』養殖場 / 〈C〉(海・川などの)『床』,水底 / 〈C〉地層;(一般に)土台 / …‘に'寝床を与える / 〈子供など〉'を'寝かしつける / 《古》寝る,床につく
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/12/01 15:37:38」(JST)
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This article provides insufficient context for those unfamiliar with the subject. Please help improve the article with a good introductory style. (October 2009) |
Mitochondrial cytochrome bc1 complex
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Identifiers |
Symbol |
Cytochrom_B_N |
Pfam |
PF00033 |
InterPro |
IPR005797 |
PROSITE |
PDOC00171 |
SCOP |
3bcc |
SUPERFAMILY |
3bcc |
TCDB |
3.D.3 |
OPM superfamily |
3 |
OPM protein |
3h1j |
CDD |
cd00284 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
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Cytochrome b is the main subunit of transmembrane cytochrome bc1 and b6f complexes.[1][2]
Contents
- 1 Function
- 2 Structure
- 3 Use in phylogenetics
- 4 Clinical significance
- 5 Human genes
- 6 References
- 7 External links
Function
In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III (EC 1.10.2.2) - also known as the bc1 complex or ubiquinol-cytochrome c reductase. In plant chloroplasts and cyanobacteria, there is an analogous protein, cytochrome b6, a component of the plastoquinone-plastocyanin reductase (EC 1.10.99.1), also known as the b6f complex. These complexes are involved in electron transport, pumping of protons to the create a PMF. The proton gradient is finally used for the generation of ATP. Concluding, the complexes play a vital part in cells.[3]
Structure
Cytochrome b/b6[4][5] is an integral membrane protein of approximately 400 amino acid residues that probably has 8 transmembrane segments. In plants and cyanobacteria, cytochrome b6 consists of two subunits encoded by the petB and petD genes. Cytochrome b/b6 non-covalently binds two heme groups, known as b562 and b566. Four conserved histidine residues are postulated to be the ligands of the iron atoms of these two heme groups.
Use in phylogenetics
Cytochrome b is commonly used as a region of mitochondrial DNA for determining phylogenetic relationships between organisms, due to its sequence variability. It is considered to be most useful in determining relationships within families and genera. Comparative studies involving cytochrome b have resulted in new classification schemes and have been used to assign newly described species to a genus as well as to deepen the understanding of evolutionary relationships.[6]
Clinical significance
Mutations in cytochrome b primarily result in exercise intolerance in human patients; though more rare, severe multi-system pathologies have also been reported.[7]
Single-point mutations in cytochrome b of Plasmodium falciparum and P. berghei are associated with resistance to the anti-malarial drug atovaquone.[8]
Human genes
Human genes encoding cytochrome b proteins include:
- CYB5A – cytochrome b5 type A (microsomal)
- CYB5B – cytochrome b5 type B (outer mitochondrial membrane)
- CYBASC3 – cytochrome b, ascorbate dependent 3
- MT-CYB – mitochondrially encoded cytochrome b
References
- ^ Howell N (August 1989). "Evolutionary conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis". J. Mol. Evol. 29 (2): 157–69. doi:10.1007/BF02100114. PMID 2509716.
- ^ Esposti MD, De Vries S, Crimi M, Ghelli A, Patarnello T, Meyer A (July 1993). "Mitochondrial cytochrome b: evolution and structure of the protein". Biochim. Biophys. Acta 1143 (3): 243–71. doi:10.1016/0005-2728(93)90197-N. PMID 8329437.
- ^ Blankenship, Robert (2009). Molecular Mechanisms of Photosynthesis. Blackwell Publishing. pp. 124–132.
- ^ Howell N (1989). "Evolutionary conservation of protein regions in the protonmotive cytochrome b and their possible roles in redox catalysis". J. Mol. Evol. 29 (2): 157–169. doi:10.1007/BF02100114. PMID 2509716.
- ^ Esposti MD, Crimi M, Ghelli A, Patarnello T, Meyer A, De Vries S (1993). "Mitochondrial cytochrome b: evolution and structure of the protein". Biochim. Biophys. Acta 1143 (3): 243–271. doi:10.1016/0005-2728(93)90197-N. PMID 8329437.
- ^ Castresana, J. (2001). "Cytochrome b Phylogeny and the Taxonomy of Great Apes and Mammals". Molecular Biology and Evolution 18 (4): 465–471. doi:10.1093/oxfordjournals.molbev.a003825. PMID 11264397.
- ^ Blakely EL, Mitchell AL, Fisher N, Meunier B, Nijtmans LG, Schaefer AM, Jackson MJ, Turnbull DM, Taylor RW (July 2005). "A mitochondrial cytochrome b mutation causing severe respiratory chain enzyme deficiency in humans and yeast". FEBS J. 272 (14): 3583–92. doi:10.1111/j.1742-4658.2005.04779.x. PMID 16008558.
- ^ Siregar JE, Syafruddin D, Matsuoka H, Kita K, Marzuki S (June 2008). "Mutation underlying resistance of Plasmodium berghei to atovaquone in the quinone binding domain 2 (Qo(2)) of the cytochrome b gene". Parasitology International 57 (2): 229–32. doi:10.1016/j.parint.2007.12.002. PMID 18248769.
External links
- Cytochromes b at the US National Library of Medicine Medical Subject Headings (MeSH)
Proteins: hemeproteins
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Globins |
Hemoglobin |
Subunits |
Alpha locus on 16: |
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Beta locus on 11: |
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Tetramers |
stages of development: |
Embryonic
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- HbE Gower 1 (ζ2ε2)
- HbE Gower 2 (α2ε2)
- HbE Portland I (ζ2γ2)
- HbE Portland II (ζ2β2)
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Fetal
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- HbF/Fetal (α2γ2)
- HbA (α2β2)
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Adult
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- HbA (α2β2)
- HbA2 (α2δ2)
- HbF/Fetal (α2γ2)
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pathology: |
- HbH (β4)
- Barts (γ4)
- HbS (α2βS2)
- HbC (α2βC2)
- HbE (α2βE2)
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Compounds |
- Carboxyhemoglobin
- Carbaminohemoglobin
- Oxyhemoglobin/Deoxyhemoglobin
- Sulfhemoglobin
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Other human |
- Glycated hemoglobin
- Methemoglobin
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Nonhuman |
- Chlorocruorin
- Erythrocruorin
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Other |
human: |
- Myoglobin
- Neuroglobin
- Cytoglobin
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plant: |
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Other |
- Cytochrome
- Cytochrome b
- Cytochrome P450
- Hemocyanin
- Methemalbumin
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see also disorders of globin and globulin proteins
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cell/phys (coag, heme, immu, gran), csfs
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rbmg/mogr/tumr/hist, sysi/epon, btst
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drug (B1/2/3+5+6), btst, trns
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UpToDate Contents
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English Journal
- Bioinformatic identification of cytochrome b5 homologues from the parasitic nematode Ascaris suum and the free-living nematode Caenorhabditis elegans highlights the crucial role of A. suum adult-specific secretory cytochrome b5 in parasitic adaptation.
- Takamiya S1, Hashimoto M2, Mita T2, Yokota T3, Nakajima Y4, Yamakura F5, Sugio S3, Fujimura T6, Ueno T6, Yamasaki H7.
- Parasitology international.Parasitol Int.2016 Apr;65(2):113-20. doi: 10.1016/j.parint.2015.11.004. Epub 2015 Nov 10.
- We previously reported that adult Ascaris suum possesses NADH-metmyoglobin and NADH-methaemoglobin reductase systems that are located in the cells of the body wall and in the extracellular perienteric fluid, respectively, which helps them adapt to environmental hypoxia by recovering the differential
- PMID 26571414
- New ideas about genetic differentiation of Chilo suppressalis (Lepidoptera: Pyralidae) populations in China based on the mtDNA cytochrome b gene.
- Tang XT1, Zheng FS1, Lu MX1, Du YZ1.
- Mitochondrial DNA.Mitochondrial DNA.2016 Mar;27(2):1567-73. doi: 10.3109/19401736.2014.958670. Epub 2015 Sep 4.
- The striped stem borer, Chilo suppressalis (Walker), is an important pest of rice in China and other parts of the world. To further explore the population genetic structure and genetic differentiation of C. suppressalis populations found on rice in China, we amplified 432 bp fragments of the cytoc
- PMID 25211083
- Genetic structure of populations and conservation issues relating to an endangered catfish, Clarias batrachus, in India.
- Khedkar GD1,2, Tiknaik A1, Kalyankar AD1, A CS3, Khedkar CD4, Ron TB5, Haymer D2.
- Mitochondrial DNA.Mitochondrial DNA.2016 Mar;27(2):1181-7. doi: 10.3109/19401736.2014.945524. Epub 2014 Aug 8.
- The Asian catfish, Clarias batrachus (Linnaeus, 1758), is a highly valued species endemic to India that is currently in drastic decline in most of its natural habitat. The present study was undertaken to document the genetic structure of populations of this species using mitochondrial DNA markers, s
- PMID 25103426
Japanese Journal
- Nanoscale charge transport in cytochrome c
- Yamaguchi Harumasa,Che Dock-Chil,Hirano Yoshiaki,Suzuki Masayuki,Higuchi Yoshiki,Matsumoto Takuya
- Jpn. J. Appl. Phys. 54(9), 095201, 2015-08-07
- … The redox-active molecule of a cytochrome c<inf>3</inf>/DNA network exhibits nonlinear current–voltage (I–V) characteristics with a threshold bias voltage at low temperature and zero-bias conductance at room temperature. … I–V curves for the cytochrome c<inf>3</inf>/DNA network are well matched with the Coulomb blockade network model. …
- NAID 150000111304
- スラブ光導波路分光法を用いる固液界面でのチトクロームcの固定化評価と直接電子移動反応のその場観察 (有機エレクトロニクス)
- 松田 直樹,岡部 浩隆
- 電子情報通信学会技術研究報告 = IEICE technical report : 信学技報 115(68), 5-9, 2015-05-29
- NAID 40020491118
- 2,2',3,4,4',5,5'-七塩素化ビフェニル(CB180)の動物肝ミクロゾームによる代謝 (油症とPCB及びダイオキシン関連化合物に関する研究報告集(第25集))
- 太田 千穂,原口 浩一,加藤 善久 [他],遠藤 哲也,木村 治,古賀 信幸
- 福岡医学雑誌 = Fukuoka acta medica 106(5), 176-183, 2015-05-25
- … These results suggest that 3ʼ-OH-CB180 is a major metabolite and is formed by PB-inducible cytochrome P450 (CYP2B enzymes) in animals and also guinea pigs possess much higher activity to metabolize CB180 than rats and hamsters. …
- NAID 120005624046
Related Links
- シトクロム(cytochrome) シトクロム(cytochrome)とは酸化還元機能を持つヘム鉄を含有するヘムタンパク質の一種である。1886年にMacMunnによって存在が指摘され、1925年にKeilinによって酸化還元機能を持ち好気呼吸に重要な役割を ...
- Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. ... Defects in MT-CYB are a ...
Related Pictures
★リンクテーブル★
[★]
- 英
- cytochrome b
- 関
- チトクロムb
[★]
- 英
- cytochrome b
- 関
- シトクロムb
[★]
チトクロムb5還元酵素、チトクロムb5レダクターゼ、シトクロムb5還元酵素、シトクロムb5レダクターゼ
[★]
フラボチトクロムb2
- 関
- lactate flavocytochrome reductase
[★]
チトクロムb6f複合体、シトクロムb6f複合体
[★]
チトクロムb6、シトクロムb6
[★]
- Mg2+存在下でC3, B, Dが反応してC3bBbとなり、これがC3転換酵素(C3bBb)あるいはC5転換酵素(C3bBb3b)を形成する。これらはP(properdin)と結合して活性化し、それぞれC3、C5を活性化する
[★]
- 同
- bicoid遺伝子