チトクロムb6、シトクロムb6
WordNet
- (biochemistry) a class of hemoprotein whose principal biological function is electron transfer (especially in cellular respiration)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/08/08 15:39:46」(JST)
[Wiki en表示]
|
|
This article provides insufficient context for those unfamiliar with the subject. Please help improve the article with a good introductory style. (October 2009) (Learn how and when to remove this template message) |
|
Mitochondrial cytochrome bc1 complex
|
| 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 |
|
Cytochrome b is a protein found in the mitochondria of eukaryotic cells. It functions as part of the electron transport chain and 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 proton motive 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
|
|
| Globins |
| Hemoglobin |
| Subunits |
| Alpha locus on 16: |
|
|
| Beta locus on 11: |
|
|
|
| Tetramers |
| stages of development: |
| Embryonic |
- HbE Gower 1 (ζ2ε2)
- HbE Gower 2 (α2ε2)
- HbE Portland I (ζ2γ2)
- HbE Portland II (ζ2β2)
|
|
| Fetal |
- HbF/Fetal (α2γ2)
- HbA (α2β2)
|
|
| Adult |
- HbA (α2β2)
- HbA2 (α2δ2)
- HbF/Fetal (α2γ2)
|
|
|
| pathology: |
- HbH (β4)
- Barts (γ4)
- HbS (α2βS2)
- HbC (α2βC2)
- HbE (α2βE2)
|
|
|
| Compounds |
- Carboxyhemoglobin
- Carbaminohemoglobin
- Oxyhemoglobin/Deoxyhemoglobin
- Sulfhemoglobin
|
|
| Other human |
- Glycated hemoglobin
- Methemoglobin
|
|
| Nonhuman |
- Chlorocruorin
- Erythrocruorin
|
|
|
| Other |
| human: |
- Myoglobin
- Neuroglobin
- Cytoglobin
|
|
| plant: |
|
|
|
|
| Other |
- Cytochrome
- Cytochrome b
- Cytochrome P450
- Hemocyanin
- Methemalbumin
|
|
|
see also disorders of globin and globulin proteins
|
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Copper stress-induced changes in leaf soluble proteome of Cu-sensitive and tolerant Agrostis capillaris L. populations.
- Hego E1,2, Vilain S3, Barré A4, Claverol S5, Dupuy JW5, Lalanne C1,2, Bonneu M6, Plomion C1,2, Mench M1,2.
- Proteomics.Proteomics.2016 May;16(9):1386-97. doi: 10.1002/pmic.201500083.
- Changes in leaf soluble proteome were explored in 3-month-old plants of metallicolous (M) and nonmetallicolous (NM) Agrostis capillaris L. populations exposed to increasing Cu concentrations (1-50 μM) to investigate molecular mechanisms underlying plant responses to Cu excess and tolerance of M pl
- PMID 26900021
- Strategies for improving C4 photosynthesis.
- von Caemmerer S1, Furbank RT2.
- Current opinion in plant biology.Curr Opin Plant Biol.2016 Apr 26;31:125-134. doi: 10.1016/j.pbi.2016.04.003. [Epub ahead of print]
- Recent activities to improve photosynthetic performance in crop plants has focused mainly on C3 photosynthesis where there are clear identified targets such as improving Rubisco kinetics, installation of a CO2 concentrating mechanism and alleviating limitations in chloroplast electron transport. Her
- PMID 27127850
- Mitochondrial gene polymorphisms alter hepatic cellular energy metabolism and aggravate diet-induced non-alcoholic steatohepatitis.
- Schröder T1, Kucharczyk D2, Bär F2, Pagel R3, Derer S2, Jendrek ST3, Sünderhauf A2, Brethack AK2, Hirose M4, Möller S5, Künstner A6, Bischof J4, Weyers I7, Heeren J8, Koczan D9, Schmid SM2, Divanovic S10, Giles DA10, Adamski J11, Fellermann K2, Lehnert H2, Köhl J12, Ibrahim S4, Sina C2.
- Molecular metabolism.Mol Metab.2016 Feb 2;5(4):283-95. doi: 10.1016/j.molmet.2016.01.010. eCollection 2016.
- OBJECTIVE: Non-alcoholic fatty liver disease (NAFLD) is the most common chronic liver disease and is associated with an enhanced risk for liver and cardiovascular diseases and mortality. NAFLD can progress from simple hepatic steatosis to non-alcoholic steatohepatitis (NASH). However, the mechanisms
- PMID 27069868
Japanese Journal
- 2,2',3,4',5,5'-六塩素化ビフェニル(CB146)のin vitro代謝の動物種差
- 太田 千穂,原口 浩一,加藤 善久,遠藤 哲也,古賀 信幸,Ohta Chiho,Haraguchi Koichi,Kato Yoshihisa,Endo Tetsuya,Koga Nobuyuki,オオタ チホ,ハラグチ コウイチ,カトウ ヨシヒサ,エンドウ テツヤ,コガ ノブユキ
- 福岡医学雑誌 104(4), 161-169, 2013-04-25
- … The formation of M-1 was significantly correlated with CYP2B6 activity. … These results suggest that 3'-OH-CB146 is formed by PB-inducible cytochrome P450 (CYP2B enzymes) in animal and human livers and 4-OH-CB146 is a major metabolite in rat and human liver. …
- NAID 120005303404
- Drug Interaction Study between Bupropion and Ticlopidine in Male CF-1 Mice
- Molnari Jillissa Christine,Hassan Hazem EmadEldin,Moeller Bryant Michael [他],Myers Alan Lewis
- Biological and Pharmaceutical Bulletin 34(3), 447-451, 2011
- … Bupropion is an atypical antidepressant that is biotransformed in humans to its major active metabolite hydroxybupropion by cytochrome P450 2B6 (CYP2B6). … Co-administration of bupropion with an inhibitor of CYP2B6 can result in a serious drug interaction, leading to bupropion related adverse effects (e.g. seizures). … Our findings support future in vivo drug interaction studies in mice between bupropion and CYP2B6 inhibitors. …
- NAID 130000657830
- High expression of the mRNA of cytochrome P450 and phase II enzymes in the lung and kidney tissues of cattle
- Darwish W. S.,Ikenaka Y.,El-Ghareeb W. R.,Ishizuka M.
- Animal 4(12), 2023-2029, 2010-12-01
- … The objective of this study was to investigate the tissue-specific mRNA expression of different cytochrome P450 (CYP) isoforms, UDP glucuronsyl transferase 1A1 (UGT1A1) and glutathione-S-transferase (GSTA1) in the different tissues (liver, mammary gland, lungs, spleen, kidney cortex, heart, masseter muscle and tongue) of cattle, using quantitative real-time polymerase chain reaction (qPCR). …
- NAID 80021378126
Related Links
- This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also ...
- Enables the directed movement of electrons within the cytochrome b6/f complex of photosystem II. 2008-05-12 Deleted DEFINITION Enables the directed movement of electrons within the cytochrome b6/f complex of photosystem ...
Related Pictures
★リンクテーブル★
[★]
- 英
- cytochrome b6
- 関
- チトクロムb6
[★]
- 英
- cytochrome b6
- 関
- シトクロムb6
[★]
チトクロムb6f複合体、シトクロムb6f複合体