肌红蛋白 - 维基百科，自由的百科全书

肌红蛋白
	肌红蛋白的螺旋结构域模型
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	3RGK
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
基因本体论描述
分子功能	· oxygen transporter activity; · oxygen binding; · heme binding; · metal ion binding;
生物过程	· response to hypoxia; · transport; · heart development; · response to hormone stimulus; · slow-twitch skeletal muscle fiber contraction; · response to hydrogen peroxide; · enucleate erythrocyte differentiation; · brown fat cell differentiation;
	Sources: Amigo / QuickGO
RNA表达模式
	更多表达数据
直系同源体
	查; 论; 编;

肌红蛋白（英語：Myoglobin; Mb; MB），又稱肌紅素，是由153个胺基酸环绕中央的血基質组成的单链蛋白质。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儲存氧气的功能。因為只需要一點氧分壓便可以使其對氧氣的結合力達到飽和，所以比血红蛋白更適合儲存氧氣。血基質對一氧化碳的親和力比氧氣大20,000倍，但是因為肌紅蛋白三級結構上His64（His E7）胺基酸不但可以與氧氣產生氫鍵還可以使一氧化碳偏離原來的結合時的自然狀態，在這一來一往的情形下，使得肌紅蛋白對一氧化碳的親和力只比氧氣高出200倍。由於不具有四級構造，所以不像血紅素一樣，產生協同效應。

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。

參考文獻[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.

延伸閱讀[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）

外部參考[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可用的所有結構信息之概述：P02144 (Human Myoglobin) 在PDBe-KB（英语：PDBe-KB）。

[pmid845960-1] 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.

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