- 同
- SOD
WordNet
- the univalent anion O2-; "much of the O2 supporting cellular respiration is reduced to the superoxide anion O2-" (同)superoxide_anion
- a metallic oxide containing the univalent anion O2-
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/04/28 16:55:54」(JST)
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Structure of a human Mn superoxide dismutase 2 tetramer.[1]
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| EC number | 1.15.1.1 | ||||||||
| CAS number | 9054-89-1 | ||||||||
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| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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Superoxide dismutases (SOD, EC 1.15.1.1) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2−) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2−).
Contents
- 1 Chemical Reaction
- 2 Types
- 2.1 General
- 2.2 Human
- 3 Plants
- 4 Bacteria
- 5 Biochemistry
- 6 Physiology
- 7 Role in disease
- 8 Pharmacological activity
- 9 Cosmetic uses
- 10 Commercial sources
- 11 See also
- 12 References
- 13 External links
Chemical Reaction
SOD enzymes deal with the superoxide radical by alternately adding or removing an electron from the superoxide molecules it encounters, thus changing the O2− into one of two less damaging species: either molecular oxygen (O2) or hydrogen peroxide (H2O2). This SOD-catalyzed dismutation of superoxide may be written, for Cu,Zn SOD, with the following half-reactions :
- Cu2+-SOD + O2− → Cu+-SOD + O2
- Cu+-SOD + O2− + 2H+ → Cu2+-SOD + H2O2
The general form, applicable to all the different metal-coordinated forms of SOD, can be written as follows:
- M(n+1)+-SOD + O2− → Mn+-SOD + O2
- Mn+-SOD + O2− + 2H+ → M(n+1)+-SOD + H2O2.
where M = Cu (n=1) ; Mn (n=2) ; Fe (n=2) ; Ni (n=2).
In a series of such reactions, the oxidation state and the charge of the metal cation oscillates between n and n+1: +1 and +2 for Cu, or +2 and +3 for the other metals .
Types
General
Bovine Cu-Zn SOD subunit.[2]
Irwin Fridovich and Joe McCord at Duke University discovered the enzymatic activity of superoxide dismutase in 1968.[3] SODs were previously known as a group of metalloproteins with unknown function; for example, CuZnSOD was known as erythrocuprein (or hemocuprein, or cytocuprein) or as the veterinary anti-inflammatory drug "Orgotein".[4] Likewise, Brewer (1967) identified a protein that later became known as superoxide dismutase as an indophenol oxidase by protein analysis of starch gels using the phenazine-tetrazolium technique.[5]
Mn-SOD vs Fe-SOD dimers
Several common forms of SOD exist: they are proteins whose active site uses copper and zinc, or manganese, iron, or nickel. Thus, there are three major families of superoxide dismutase, depending on the protein fold and the metal cofactor: the Cu/Zn type (which binds both copper and zinc), Fe and Mn types (which bind either iron or manganese), and the Ni type, which binds nickel.
- Copper and zinc – most commonly used by eukaryotes, including humans. The cytosols of virtually all eukaryotic cells contain an SOD enzyme with copper and zinc (Cu-Zn-SOD). For example, Cu-Zn-SOD available commercially is normally purified from bovine red blood cells. The bovine Cu-Zn enzyme is a homodimer of molecular weight 32,500. It was the first SOD whose atomic-detail crystal structure was solved, in 1975.[6] It is an 8-stranded "Greek key" beta-barrel, with the active site held between the barrel and two surface loops. The two subunits are tightly joined back-to-back, mostly by hydrophobic and some electrostatic interactions. The ligands of the copper and zinc are six histidine and one aspartate side-chains; one histidine is bound between the two metals.[7]
- Iron or manganese – used by prokaryotes and protists, and in mitochondria
- Iron – E. coli and many other bacteria also contain a form of the enzyme with iron (Fe-SOD); some bacteria contain Fe-SOD, others Mn-SOD, and some contain both (e.g., "E. coli"). Fe-SOD can be found in the chloroplasts of plants. The 3D structures of the homologous Mn and Fe superoxide dismutases have the same arrangement of alpha-helices, and their active sites contain the same type and arrangement of amino acid side-chains. They are usually dimers, but occasionally tetramers.
Active site of Human Manganese SOD. Manganese shown in purple. [8]
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- Manganese – Chicken liver (and nearly all other) mitochondria, and many bacteria (such as E. coli), contain a form with manganese (Mn-SOD): For example, the Mn-SOD found in human mitochondria. The ligands of the manganese ions are 3 histidine side-chains, an aspartate side-chain and a water molecule or hydroxy ligand, depending on the Mn oxidation state (respectively II and III).[9]
- Nickel – prokaryotic. This has a hexameric (6-copy) structure built from right-handed 4-helix bundles, each containing N-terminal hooks that chelate a Ni ion. The Ni-hook contains the motif His-Cys-X-X-Pro-Cys-Gly-X-Tyr; it provides most of the interactions critical for metal binding and catalysis and is, therefore, a likely diagnostic of NiSODs.[10][11]
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In higher plants, SOD isozymes have been localized in different cell compartments. Mn-SOD is present in mitochondria and peroxisomes. Fe-SOD has been found mainly in chloroplasts but has also been detected in peroxisomes, and CuZn-SOD has been localized in cytosol, chloroplasts, peroxisomes, and apoplast.[13][14]
Human
Three forms of superoxide dismutase are present in humans, in all other mammals, and most chordates. SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. The first is a dimer (consists of two units), whereas the others are tetramers (four subunits). SOD1 and SOD3 contain copper and zinc, whereas SOD2, the mitochondrial enzyme, has manganese in its reactive centre. The genes are located on chromosomes 21, 6, and 4, respectively (21q22.1, 6q25.3 and 4p15.3-p15.1).
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Plants
In higher plants, superoxide dismutase enzymes (SODs) act as antioxidants and protect cellular components from being oxidized by reactive oxygen species (ROS).[17] ROS can form as a result of drought, injury, herbicides and pesticides, ozone, plant metabolic activity, nutrient deficiencies, photoinhibition, temperature above and below ground, toxic metals, and UV or gamma rays.[18][19] To be specific, molecular O2 is reduced to O2− (an ROS called superoxide) when it absorbs an excited electron released from compounds of the electron transport chain. Superoxide is known to denature enzymes, oxidize lipids, and fragment DNA.[18] SODs catalyze the production of O2 and H2O2 from superoxide (O2−), which results in less harmful reactants.
When acclimating to increased levels of oxidative stress, SOD concentrations typically increase with the degree of stress conditions. The compartmentalization of different forms of SOD throughout the plant makes them counteract stress very effectively. There are three well-known and -studied classes of SOD metallic coenzymes that exist in plants. First, Fe SODs consist of two species, one homodimer (containing 1-2 g Fe) and one tetramer (containing 2-4 g Fe). They are thought to be the most ancient SOD metalloenzymes and are found within both prokaryotes and eukaryotes. Fe SODs are most abundantly localized inside plant chloroplasts, where they are indigenous. Second, Mn SODs consist of a homodimer and homotetramer species each containing a single Mn(III) atom per subunit. They are found predominantly in mitochondrion and peroxisomes. Third, Cu-Zn SODs have electrical properties very different from those of the other two classes. These are concentrated in the chloroplast, cytosol, and in some cases the extracellular space. Note that Cu-Zn SODs provide less protection than Fe SODs when localized in the chloroplast.[17][18][19]
Bacteria
Human white blood cells generate superoxide and other reactive oxygen species to kill bacteria. During infection, some bacteria (e.g., Burkholderia pseudomallei) therefore produce superoxide dismutase to protect themselves from being killed.[20]
Biochemistry
SOD out-competes damaging reactions of superoxide, thus protecting the cell from superoxide toxicity. The reaction of superoxide with non-radicals is spin-forbidden. In biological systems, this means that its main reactions are with itself (dismutation) or with another biological radical such as nitric oxide (NO) or with a transition-series metal. The superoxide anion radical (O2−) spontaneously dismutes to O2 and hydrogen peroxide (H2O2) quite rapidly (~105 M−1s−1 at pH 7). SOD is necessary because superoxide reacts with sensitive and critical cellular targets. For example, it reacts with the NO radical, and makes toxic peroxynitrite.
Because the uncatalysed dismutation reaction for superoxide requires two superoxide molecules to react with each other, the dismutation rate is second-order with respect to initial superoxide concentration. Thus, the half-life of superoxide, although very short at high concentrations (e.g., 0.05 seconds at 0.1mM) is actually quite long at low concentrations (e.g., 14 hours at 0.1 nM). In contrast, the reaction of superoxide with SOD is first order with respect to superoxide concentration. Moreover, superoxide dismutase has the largest kcat/KM (an approximation of catalytic efficiency) of any known enzyme (~7 x 109 M−1s−1),[21] this reaction being limited only by the frequency of collision between itself and superoxide. That is, the reaction rate is "diffusion-limited".
The high efficiency of superoxide dismutase seems necessary: even at the subnanomolar concentrations achieved by the high concentrations of SOD within cells, superoxide inactivates the citric acid cycle enzyme aconitase, can poison energy metabolism, and releases potentially toxic iron. Aconitase is one of several iron-sulfur-containing (de)hydratases in metabolic pathways shown to be inactivated by superoxide.[22]
Physiology
Superoxide is one of the main reactive oxygen species in the cell. As a consequence, SOD serves a key antioxidant role. The physiological importance of SODs is illustrated by the severe pathologies evident in mice genetically engineered to lack these enzymes. Mice lacking SOD2 die several days after birth, amid massive oxidative stress.[23] Mice lacking SOD1 develop a wide range of pathologies, including hepatocellular carcinoma,[24] an acceleration of age-related muscle mass loss,[25] an earlier incidence of cataracts and a reduced lifespan. Mice lacking SOD3 do not show any obvious defects and exhibit a normal lifespan, though they are more sensitive to hyperoxic injury.[26] Knockout mice of any SOD enzyme are more sensitive to the lethal effects of superoxide-generating drugs, such as paraquat and diquat.
Drosophila lacking SOD1 have a dramatically shortened lifespan, whereas flies lacking SOD2 die before birth. SOD knockdowns in C. elegans do not cause major physiological disruptions. Knockout or null mutations in SOD1 are highly detrimental to aerobic growth in the yeast Sacchormyces cerevisiae and result in a dramatic reduction in post-diauxic lifespan. SOD2 knockout or null mutations cause growth inhibition on respiratory carbon sources in addition to decreased post-diauxic lifespan.
Several prokaryotic SOD null mutants have been generated, including E. Coli. The loss of periplasmic CuZnSOD causes loss of virulence and might be an attractive target for new antibiotics.
Role in disease
Mutations in the first SOD enzyme (SOD1) can cause familial amyotrophic lateral sclerosis (ALS, a form of motor neuron disease).[27][28][29][30] The most common mutation in the U.S. is A4V, while the most intensely studied is G93A. The other two isoforms of SOD have not been linked to any human diseases, however, in mice inactivation of SOD2 causes perinatal lethality[23] and inactivation of SOD1 causes hepatocellular carcinoma.[24] Mutations in SOD1 can cause familial ALS (several pieces of evidence also show that wild-type SOD1, under conditions of cellular stress, is implicated in a significant fraction of sporadic ALS cases, which represent 90% of ALS patients.),[31] by a mechanism that is presently not understood, but not due to loss of enzymatic activity or a decrease in the conformational stability of the SOD1 protein. Overexpression of SOD1 has been linked to the neural disorders seen in Down syndrome.[32]
In mice, the extracellular superoxide dismutase (SOD3, ecSOD) contributes to the development of hypertension.[33][34] Diminished SOD3 activity has been linked to lung diseases such as Acute Respiratory Distress Syndrome (ARDS) or Chronic obstructive pulmonary disease (COPD).[35][36][37]
Superoxide dismutase is also not expressed in neural crest cells in the developing fetus. Hence, high levels of free radicals can cause damage to them and induce dysraphic anomalies (neural tube defects).
Pharmacological activity
SOD has powerful antinflammatory activity. For example, SOD is a highly effective experimental treatment of chronic inflammation in colitis[citation needed]. Treatment with SOD decreases reactive oxygen species generation and oxidative stress and, thus, inhibits endothelial activation and indicate that modulation of factors that govern adhesion molecule expression and leukocyte-endothelial interactions. Therefore, such antioxidants may be important new therapies for the treatment of inflammatory bowel disease.[38]
Likewise, SOD has multiple pharmacological activities. E.g., it ameliorates cis-platinum-induced nephrotoxicity in rodents.[39] As "Orgotein" or "ontosein", a pharmacologically-active purified bovine liver SOD, it is also effective in the treatment of urinary tract inflammatory disease in man.[40] For a time, bovine liver SOD even had regulatory approval in several European countries for such use. This was truncated by concerns about prion disease.
An SOD-mimetic agent, TEMPOL, is currently in clinical trials for radioprotection and to prevent radiation-induced dermatitis.[41] TEMPOL and similar SOD-mimetic nitroxides exhibit a multiplicity of actions in diseases involving oxidative stress.[42]
Cosmetic uses
SOD may reduce free radical damage to skin—for example, to reduce fibrosis following radiation for breast cancer. Studies of this kind must be regarded as tentative, however, as there were not adequate controls in the study including a lack of randomization, double-blinding, or placebo.[43] Superoxide dismutase is known to reverse fibrosis, perhaps through reversion of myofibroblasts back to fibroblasts.[44][further explanation needed]
Commercial sources
SOD is commercially obtained from bovine liver, though it is also found in yeast, spinach, and chicken liver.[45]
See also
- Catalase
- Peroxidase
- Jiaogulan
References
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- ^ PDB 2SOD;Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC (September 1982). "Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase". J. Mol. Biol. 160 (2): 181–217. doi:10.1016/0022-2836(82)90174-7. PMID 7175933.
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External links
- Online 'Mendelian Inheritance in Man' (OMIM) 105400 (ALS)
- The ALS Online Database
- A short but substantive overview of SOD and its literature.
- Damage-Based Theories of Aging Includes a discussion of the roles of SOD1 and SOD2 in aging.
- Physicians' Comm. For Responsible Med.
- SOD and Oxidative Stress Pathway Image
- Historical information on SOD research"The evolution of Free Radical Biology & Medicine: A 20-year history" and "Free Radical Biology & Medicine The last 20 years: The most highly cited papers"
- JM McCord discusses the discovery of SOD
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UpToDate Contents
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- 1. 家族性筋萎縮性側索硬化症 familial amyotrophic lateral sclerosis
- 2. 筋萎縮性側索硬化症の疫学および病因 epidemiology and pathogenesis of amyotrophic lateral sclerosis
- 3. 気管支肺異形成症の予防 prevention of bronchopulmonary dysplasia
- 4. 癌患者における膀胱炎 cystitis in patients with cancer
- 5. 筋萎縮性側索硬化症の病態修飾療法 disease modifying treatment of amyotrophic lateral sclerosis
English Journal
- Impact of Metal Nanoform Colloidal Solution on the Adaptive Potential of Plants.
- Taran N1, Batsmanova L2, Kovalenko M3, Okanenko A4.
- Nanoscale research letters.Nanoscale Res Lett.2016 Dec;11(1):89. doi: 10.1186/s11671-016-1294-z. Epub 2016 Feb 15.
- Nanoparticles are a known cause of oxidative stress and so induce antistress action. The latter property was the purpose of our study. The effect of two concentrations (120 and 240 mg/l) of nanoform biogenic metal (Ag, Cu, Fe, Zn, Mn) colloidal solution on antioxidant enzymes, superoxide dismutase
- PMID 26876039
- Oxidative Damage and Energy Metabolism Disorder Contribute to the Hemolytic Effect of Amorphous Silica Nanoparticles.
- Jiang L1,2, Yu Y3,4, Li Y5,6, Yu Y7,8, Duan J9,10, Zou Y11,12, Li Q13,14, Sun Z15,16.
- Nanoscale research letters.Nanoscale Res Lett.2016 Dec;11(1):57. doi: 10.1186/s11671-016-1280-5. Epub 2016 Feb 2.
- Amorphous silica nanoparticles (SiNPs) have been extensively used in biomedical applications due to their particular characteristics. The increased environmental and iatrogenic exposure of SiNPs gained great concerns on the biocompatibility and hematotoxicity of SiNPs. However, the studies on the he
- PMID 26831695
- Antioxidant Activity of Heracleum persicum Fruit Extract: Evidence from a Randomized Controlled Trial.
- Panahi Y1, Dadjou Y2, Pishgoo B2, Akbari A2, Sahebkar A3,4.
- Journal of dietary supplements.J Diet Suppl.2016 Sep 2;13(5):530-7. doi: 10.3109/19390211.2015.1120842. Epub 2016 Jan 28.
- Oxidative stress is a unifying feature of several cardiometabolic risk factors, and has been suggested to be implicated in atherogenesis. This study aimed to investigate the efficacy of supplementation with Heracleum persicum fruit-a common dietary spice-in modulating systemic biomarkers of oxidativ
- PMID 26820395
Japanese Journal
- Systemic Oxidative Stress Is Associated With Lower Aerobic Capacity and Impaired Skeletal Muscle Energy Metabolism in Patients With Metabolic Syndrome
- Yokota Takashi,Kinugawa Shintaro,Yamato Mayumi,Hirabayashi Kagami,Suga Tadashi,Takada Shingo,Harada Kuniaki,Morita Noriteru,Oyama-Manabe Noriko,Kikuchi Yasuka,Okita Koichi,Tsutsui Hiroyuki
- Diabetes Care 36(5), 1341-1346, 2013-05-00
- … Systemic lipid peroxidation was assessed by serum thiobarbituric acid reactive substances (TBARS), and systemic antioxidant defense capacity was assessed by serum total thiols and enzymatic activity of superoxide dismutase (SOD). …
- NAID 120005311817
- 最新原著レビュー 細胞質のスーパーオキサイドは低骨代謝回転型骨量減少と加齢性コラーゲン架橋変化を引き起こし骨脆弱化させる
- 野尻 英俊
- 整形外科 = Orthopedic surgery 64(1), 89-92, 2013-01-00
- NAID 40019538687
- Aromatic constituents of Cymbidium Great Flower Marie Laurencin and their antioxidative activity
- Yoshikawa Kazuko,Otsu Misa,Ito Takuya [他]
- Journal of natural medicines 67(1), 217-221, 2013-00-00
- NAID 40019527967
Related Links
- Find patient medical information for SUPEROXIDE DISMUTASE on WebMD including its uses, effectiveness, side effects and safety, interactions, user ratings and products that have it. ... Superoxide dismutase is an enzyme found ...
- Additional reading on superoxide dismutase P. Pasinelli and R. H. Brown (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nature Reviews Neuroscience 7, 710-721. J. A. Imlay and I. Fridovich ...
Related Pictures
★リンクテーブル★
| リンク元 | 「スーパーオキシドジスムターゼ」「スーパーオキシドディスムターゼ」「SOD」 |
| 拡張検索 | 「manganese superoxide dismutase」「Cu-Zn superoxide dismutase」「copper-zinc superoxide dismutase」 |
| 関連記事 | 「dismutase」「superoxide」 |
「スーパーオキシドジスムターゼ」
- 英
- superoxide dismutase, SOD
- 同
- スーパーオキサイドジスムターゼ、超酸化物不均化酵素
- 関
- [[]]
O2.- + 2H+ → H2O2 + O2
ペルオキシダーゼと並んで抗酸化酵素の一つ セルオキシソームに局在。 ４量体 サブユニットに１つ鉄イオンが含まれている。
生物種とSOD
Cu-SOD, Zn-SOD 高等動植物の細胞質 EC-SOD(A,B,C) 高等動物の体液と血管表面 Mn-SOD 高等動植物のミトコンドリアと細菌
「スーパーオキシドディスムターゼ」
スーパーオキシドディスムターゼ : 約 16,400 件 スーパーオキシドジスムターゼ : 約 47,900 件
「SOD」
「manganese superoxide dismutase」
マンガンスーパーオキシドジスムターゼ、マンガンスーパーオキサイドジスムターゼ
「Cu-Zn superoxide dismutase」
「copper-zinc superoxide dismutase」
銅・亜鉛スーパーオキシドジスムターゼ、銅・亜鉛スーパーオキサイドジスムターゼ