Sitokrom c oksidase: Perbedaan antara revisi
Tampilan
Konten dihapus Konten ditambahkan
k r2.7.2+) (Robot: Mengubah fa:سیتوکروم اکسیداز menjadi fa:سیتوکروم اکسیداز سی |
k →Rujukan: pembersihan kosmetika dasar |
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(8 revisi perantara oleh 6 pengguna tidak ditampilkan) | |||
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[[Berkas:Cytochrome_C_Oxidase_1OCC_in_Membrane_2.png|jmpl|ka|200px|Struktur kristal sitokrom c oksidase]] |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/9694260 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/9694260 |
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| title = Transcriptional regulation of mammalian cytochrome c oxidase genes |
| title = Transcriptional regulation of mammalian cytochrome c oxidase genes |
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| accessdate = 2010-11-14 |
| accessdate = 2010-11-14 |
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| work = Center for Molecular Medicine and Genetics, Wayne State University School of Medicine; Grossman LI, Seelan RS, Jaradat SA. |
| work = Center for Molecular Medicine and Genetics, Wayne State University School of Medicine; Grossman LI, Seelan RS, Jaradat SA. |
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}}</ref> dan 10 buah pada [[DNA]] dalam [[inti sel]] [[eukariota]].<ref>{{en}}{{cite web |
}}</ref> dan 10 buah pada [[DNA]] dalam [[inti sel]] [[eukariota]].<ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/16760263 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/16760263 |
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| title = Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process |
| title = Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process |
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| accessdate = 2010-11-14 |
| accessdate = 2010-11-14 |
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| work = Departments of Neurology, The John T. Macdonald Foundation Center for Medical Genetics, University of Miami Miller School of Medicine; Fontanesi F, Soto IC, Horn D, Barrientos A. |
| work = Departments of Neurology, The John T. Macdonald Foundation Center for Medical Genetics, University of Miami Miller School of Medicine; Fontanesi F, Soto IC, Horn D, Barrientos A. |
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}}</ref> [[ |
}}</ref> [[ekspresi gen]]etik pada [[hepatosit]] [[hewan]] [[sapi]] adalah: |
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* 5 [[fosfatidil etanolamina]] |
* 5 [[fosfatidil etanolamina]] |
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* 3 [[fosfatidil gliserol]] |
* 3 [[fosfatidil gliserol]] |
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* 1 [[magnesium|Mg]] |
* 1 [[magnesium|Mg]] |
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* 1 [[seng|Zn]] |
* 1 [[seng|Zn]] |
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dengan 2 [[kanal proton]] yang terbentang dari matriks [[mitokondria]] menuju [[sitoplasma]].<ref>{{en}}{{cite web |
dengan 2 [[kanal proton]] yang terbentang dari matriks [[mitokondria]] menuju [[sitoplasma]].<ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/8638158 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/8638158 |
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| title = The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A |
| title = The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A |
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* cyt.c adalah [[sitokrom c]] |
* cyt.c adalah [[sitokrom c]] |
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Pada lintasan D, setelah molekul O<sub>2</sub> terikat pada situs reduksi yang berupa kompleks Fe<sup>2+</sup>(a3) dan Cu(B), O<sub>2</sub> segera tereduksi menjadi O<sub>2</sub><sup>-</sup> dan membentuk [[ikatan hidrogen]] dengan CN<sup>-</sup> dan [[gugus fungsional|gugus]] [[hidroksil|OH<sup>-</sup>]] [[tirosina|Tyr244]] hingga memungkinkan O<sub>2</sub><sup>-</sup> menerima 3 tambahan elektron dari Cu1B<sup>+</sup>, Fe<sup>3+</sup>(a3), dan Tyr-OH,<ref>{{en}}{{cite web |
Pada lintasan D, setelah molekul O<sub>2</sub> terikat pada situs reduksi yang berupa kompleks Fe<sup>2+</sup>(a3) dan Cu(B), O<sub>2</sub> segera tereduksi menjadi O<sub>2</sub><sup>-</sup> dan membentuk [[ikatan hidrogen]] dengan CN<sup>-</sup> dan [[gugus fungsional|gugus]] [[hidroksil|OH<sup>-</sup>]] [[tirosina|Tyr244]] hingga memungkinkan O<sub>2</sub><sup>-</sup> menerima 3 tambahan elektron dari Cu1B<sup>+</sup>, Fe<sup>3+</sup>(a3), dan Tyr-OH,<ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/20385840 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/20385840 |
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| title = Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate |
| title = Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate |
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| accessdate = 2010-11-15 |
| accessdate = 2010-11-15 |
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| work = Department of Life Science, University of Hyogo; Muramoto K, Ohta K, Shinzawa-Itoh K, Kanda K, Taniguchi M, Nabekura H, Yamashita E, Tsukihara T, Yoshikawa S. |
| work = Department of Life Science, University of Hyogo; Muramoto K, Ohta K, Shinzawa-Itoh K, Kanda K, Taniguchi M, Nabekura H, Yamashita E, Tsukihara T, Yoshikawa S. |
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}}</ref> di bawah regulasi [[histidina]].<ref name="PM16829226">{{en}}{{cite web |
}}</ref> di bawah regulasi [[histidina]].<ref name="PM16829226">{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/16829226 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/16829226 |
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| title = Reaction mechanism of bovine heart cytochrome c oxidase |
| title = Reaction mechanism of bovine heart cytochrome c oxidase |
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| accessdate = 2010-11-15 |
| accessdate = 2010-11-15 |
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| work = Department of Life Science, University of Hyogo; Yoshikawa S, Muramoto K, Shinzawa-Itoh K, Aoyama H, Tsukihara T, Ogura T, Shimokata K, Katayama Y, Shimada H. |
| work = Department of Life Science, University of Hyogo; Yoshikawa S, Muramoto K, Shinzawa-Itoh K, Aoyama H, Tsukihara T, Ogura T, Shimokata K, Katayama Y, Shimada H. |
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}}</ref> Keempat elektron tersebut berasal dari [[sitokrom c|Fe<sup>2+</sup>(c)]].<ref name="PM12765763">{{en}}{{cite web |
}}</ref> Keempat elektron tersebut berasal dari [[sitokrom c|Fe<sup>2+</sup>(c)]].<ref name="PM12765763">{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/12765763 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/12765763 |
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| title = Water-gated mechanism of proton translocation by cytochrome c oxidase |
| title = Water-gated mechanism of proton translocation by cytochrome c oxidase |
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| accessdate = 2010-11-15 |
| accessdate = 2010-11-15 |
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| work = Helsinki Bioenergetics Group, Institute of Biotechnology and Biocentrum Helsinki, University of Helsinki; Wikström M, Verkhovsky MI, Hummer G. |
| work = Helsinki Bioenergetics Group, Institute of Biotechnology and Biocentrum Helsinki, University of Helsinki; Wikström M, Verkhovsky MI, Hummer G. |
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}}</ref> Pasokan [[ion]] [[hidrogen|H<sup>+</sup>]] dibawa oleh kluster 5 [[molekul]] air,<ref>{{en}}{{cite web |
}}</ref> Pasokan [[ion]] [[hidrogen|H<sup>+</sup>]] dibawa oleh kluster 5 [[molekul]] air,<ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/17309257 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/17309257 |
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| title = Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: identification of a protonated water cluster |
| title = Storage of an excess proton in the hydrogen-bonded network of the d-pathway of cytochrome C oxidase: identification of a protonated water cluster |
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Baris 59: | Baris 61: | ||
}}</ref> dari [[asam glutamat|Glu286]] di dalam matriks, untuk mereduksi [[oksigen|O<sub>2</sub>]] tersebut menjadi [[air|H<sub>2</sub>O]]. Setelah oksigen selesai tereduksi, kelebihan ion H<sup>+</sup> akan dihantarkan ke gugus [[delta-propionat]] dari Fe<sup>2+</sup>(a3). |
}}</ref> dari [[asam glutamat|Glu286]] di dalam matriks, untuk mereduksi [[oksigen|O<sub>2</sub>]] tersebut menjadi [[air|H<sub>2</sub>O]]. Setelah oksigen selesai tereduksi, kelebihan ion H<sup>+</sup> akan dihantarkan ke gugus [[delta-propionat]] dari Fe<sup>2+</sup>(a3). |
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Sifat [[hidrofobik]] gugus [[delta-propionat]] dan ikatan hidrogen yang dibentuknya dengan senyawa [[asam aspartat|Asp51]] yang terletak pada ruang antarmembran memungkinkan letupan ion H<sup>+</sup> dari gugus tersebut sebagai reaksi oksidasi, dengan reaksi reduksi Asp51 menjadi [[asparagina]].<ref name="PM16829226" /><ref>{{en}}{{cite web |
Sifat [[hidrofobik]] gugus [[delta-propionat]] dan ikatan hidrogen yang dibentuknya dengan senyawa [[asam aspartat|Asp51]] yang terletak pada ruang antarmembran memungkinkan letupan ion H<sup>+</sup> dari gugus tersebut sebagai reaksi oksidasi, dengan reaksi reduksi Asp51 menjadi [[asparagina]].<ref name="PM16829226" /><ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/16904626 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/16904626 |
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| title = Proton pumping mechanism of bovine heart cytochrome c oxidase |
| title = Proton pumping mechanism of bovine heart cytochrome c oxidase |
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| accessdate = 2010-11-15 |
| accessdate = 2010-11-15 |
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| work = Department of Life Science, University of Hyogo; Yoshikawa S, Muramoto K, Shinzawa-Itoh K, Aoyama H, Tsukihara T, Shimokata K, Katayama Y, Shimada H. |
| work = Department of Life Science, University of Hyogo; Yoshikawa S, Muramoto K, Shinzawa-Itoh K, Aoyama H, Tsukihara T, Shimokata K, Katayama Y, Shimada H. |
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}}</ref> 4 [[ion]] [[hidrogen|H<sup>+</sup>]] diletupkan dengan [[daya]] sebesar 635 [[watt|meV]],<ref>{{en}}{{cite web |
}}</ref> 4 [[ion]] [[hidrogen|H<sup>+</sup>]] diletupkan dengan [[daya]] sebesar 635 [[watt|meV]],<ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/14871119 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/14871119 |
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| title = Electrostatic study of the proton pumping mechanism in bovine heart cytochrome C oxidase |
| title = Electrostatic study of the proton pumping mechanism in bovine heart cytochrome C oxidase |
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| accessdate = 2010-11-15 |
| accessdate = 2010-11-15 |
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| work = Department of Chemistry, University of California-Davis; Popović DM, Stuchebrukhov AA. |
| work = Department of Chemistry, University of California-Davis; Popović DM, Stuchebrukhov AA. |
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}}</ref> untuk 1 molekul O<sub>2</sub> pada [[pH]] sekitar 8, namun mekanisme peletupan tersebut lenyap pada pH sekitar 10,5.<ref>{{en}}{{cite web |
}}</ref> untuk 1 molekul O<sub>2</sub> pada [[pH]] sekitar 8, namun mekanisme peletupan tersebut lenyap pada pH sekitar 10,5.<ref>{{en}} {{cite web |
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| url = http://www.ncbi.nlm.nih.gov/pubmed/19344748 |
| url = http://www.ncbi.nlm.nih.gov/pubmed/19344748 |
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| title = Internal charge transfer in cytochrome c oxidase at a limited proton supply: proton pumping ceases at high pH |
| title = Internal charge transfer in cytochrome c oxidase at a limited proton supply: proton pumping ceases at high pH |
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{{Enzim}} |
{{Enzim}} |
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[[Kategori:Enzim]] |
[[Kategori:Enzim]] |
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[[ca:Citocrom c oxidasa]] |
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[[cs:Cytochrom c oxidáza]] |
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[[de:Cytochrom-c-Oxidase]] |
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[[en:Cytochrome c oxidase]] |
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[[es:Citocromo c oxidasa]] |
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[[fa:سیتوکروم اکسیداز سی]] |
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[[fr:Cytochrome c oxydase]] |
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[[it:Citocromo-c ossidasi]] |
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[[ja:シトクロムcオキシダーゼ]] |
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[[pl:Oksydaza cytochromu c]] |
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[[pt:Citocromo c oxidase]] |
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[[ru:Цитохром с-оксидаза]] |
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[[sr:Citohrom c oksidaza]] |
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[[sv:Cytokrom c-oxidas]] |
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[[tr:Sitokrom c oksidaz]] |
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[[zh:细胞色素c氧化酶]] |