肌红蛋白
肌红蛋白（英语：Myoglobin; Mb; MB），又称肌红素，是由153个氨基酸环绕中央的血红素组成的单链蛋白质。分子量为16,700道尔顿。其对氧气的亲合力大于血红蛋白，所以在肌肉组织中有储存氧气的功能。因为只需要一点氧分压便可以使其对氧气的结合力达到饱和，所以比血红蛋白更适合储存氧气。血红素对一氧化碳的亲和力比氧气大20,000倍，但是因为肌红蛋白三级结构上His64（His E7）氨基酸不但可以与氧气产生氢键还可以使一氧化碳偏离原来的结合时的自然状态，在这一来一往的情形下，使得肌红蛋白对一氧化碳的亲和力只比氧气高出200倍。由于不具有四级构造，所以不像血红素一样，产生协同效应。
| 肌红蛋白 | |||||||||||||
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| 标识 | |||||||||||||
| 代号 | MB; PVALB | ||||||||||||
| 扩展标识 | 遗传学：160000 鼠基因：96922 同源基因：3916 GeneCards: MB Gene | ||||||||||||
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| 直系同源体 | |||||||||||||
| 物种 | 人类 | 小鼠 | |||||||||||
| Entrez | 4151 | 17189 | |||||||||||
| Ensembl | ENSG00000198125 | ENSMUSG00000018893 | |||||||||||
| UniProt | P02144 | P04247 | |||||||||||
| mRNA序列 | NM_005368.2 | NM_001164047.1 | |||||||||||
| 蛋白序列 | NP_005359.1 | NP_001157519.1 | |||||||||||
| 基因位置 |
Chr 22: 36 – 36.03 Mb |
Chr 15: 76.85 – 76.88 Mb | |||||||||||
| PubMed查询 | [1] | [2] | |||||||||||
若严重过度运动，有可能使肌细胞溶解并导致肌红蛋白进入血液，在肾脏堵住肾小管，引起肾损伤，称为横纹肌溶解症。肌细胞溶解还会释放出大量的钾，引起高钾血症。
参考文献
编辑- ^ PDB 1MBO; Takano T. Structure of myoglobin refined at 2.0 Å resolution. II. Structure of deoxymyoglobin from sperm whale. J. Mol. Biol. March 1977, 110 (3): 569–84. PMID 845960. doi:10.1016/S0022-2836(77)80112-5.
延伸阅读
编辑- Collman JP, Boulatov R, Sunderland CJ, Fu L. Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin. Chemical Reviews. Feb 2004, 104 (2): 561–88. PMID 14871135. doi:10.1021/cr0206059.
- Reeder BJ, Svistunenko DA, Cooper CE, Wilson MT. The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxidants & Redox Signaling. Dec 2004, 6 (6): 954–66. PMID 15548893. doi:10.1089/ars.2004.6.954.
- Schlieper G, Kim JH, Molojavyi A, Jacoby C, Laussmann T, Flögel U, Gödecke A, Schrader J. Adaptation of the myoglobin knockout mouse to hypoxic stress. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. Apr 2004, 286 (4): R786–92. PMID 14656764. doi:10.1152/ajpregu.00043.2003.
- Takano T. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale. Journal of Molecular Biology. Mar 1977, 110 (3): 569–84. PMID 845960. doi:10.1016/S0022-2836(77)80112-5.
- Roy A, Sen S, Chakraborti AS. In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress. Free Radical Research. Feb 2004, 38 (2): 139–46. PMID 15104207. doi:10.1080/10715160310001638038.
- Stewart JM, Blakely JA, Karpowicz PA, Kalanxhi E, Thatcher BJ, Martin BM. Unusually weak oxygen binding, physical properties, partial sequence, autoxidation rate and a potential phosphorylation site of beluga whale (Delphinapterus leucas) myoglobin. Comparative Biochemistry and Physiology B. Mar 2004, 137 (3): 401–12. PMID 15050527. doi:10.1016/j.cbpc.2004.01.007.
- Wu G, Wainwright LM, Poole RK. Microbial globins. Advances in Microbial Physiology 47. 2003: 255–310. ISBN 9780120277476. PMID 14560666. doi:10.1016/S0065-2911(03)47005-7.
- Mirceta S, Signore AV, Burns JM, Cossins AR, Campbell KL, Berenbrink M. Evolution of mammalian diving capacity traced by myoglobin net surface charge. Science. Jun 2013, 340 (6138): 1234192. PMID 23766330. doi:10.1126/science.1234192.. Also see Proteopedia article about this finding （页面存档备份，存于互联网档案馆）
外部参考
编辑- OMIM 160000 human genetics
- The Myoglobin Protein （页面存档备份，存于互联网档案馆）
- RCSB PDB featured molecule
- Which Cut Is Older? (It's a Trick Question) （页面存档备份，存于互联网档案馆） New York Times, February 21, 2006 article regarding meat industry use of carbon monoxide to keep meat looking red.
- Stores React to Meat Reports （页面存档备份，存于互联网档案馆） New York Times, March 1, 2006 article on the use of carbon monoxide to make meat appear fresh.
- PDB中UniProt可用的所有结构信息之概述：P02144 (Human Myoglobin) 在PDBe-KB。