Myoglobin




Myoglobin
Model of helical domains in myoglobin.[1]
Available structures: 1m6c, 1m6m, 1mdn, 1mnh, 1mni, 1mnj, 1mnk, 1mno, 1mwc, 1mwd, 1myg, 1myh, 1myi, 1myj, 1pmb, 1yca, 1ycb, 2mm1
Identifiers
Symbol(s) MB; MGC13548; PVALB
External IDs OMIM: 160000 MGI: 96922 Homologene: 3916
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 4151 17189
Ensembl ENSG00000198125 ENSMUSG00000018893
Uniprot P02144 Q3UVB1
Refseq NM_005368 (mRNA)
NP_005359 (protein) 		NM_013593 (mRNA)
NP_038621 (protein)
Location Chr 22: 34.33 - 34.35 Mb Chr 15: 76.84 - 76.88 Mb
Pubmed search [1] [2]
 

Myoglobin is a MB.

Meat color

Myoglobin forms nitric oxide (true of, e.g., corned beef or cured hams). Grilled meats can also take on a pink "smoke ring" that comes from the iron binding a molecule of carbon monoxide.[6] Raw meat packed in a carbon monoxide atmosphere also shows this same pink "smoke ring" due to the same molecular process. Notably, the surface of the raw meat also displays the nice pink color, which is usually associated in consumers' minds with fresh meat. This artificially-induced pink color can persist in the meat for a very long time, reportedly up to one year. [7] Hormel and Cargill are both reported to use this meat-packing process, and meat treated this way has been in the consumer market since 2003. [8] Myoglobin is found in Type I muscle, Type II A and Type II B, but most texts consider myoglobin to not be found in smooth muscle.

Role in disease

Myoglobin is released from damaged muscle tissue (rhabdomyolysis), which has very high concentrations of myoglobin. The released myoglobin is filtered by the kidneys but is toxic to the renal tubular epithelium and so may cause acute renal failure.[9]

Myoglobin is a sensitive marker for muscle injury, making it a potential marker for heart attack in patients with chest pain.[10] Its lack of specificity and the cost of the analysis has prevented its widespread use.

Structure and bonding

Myoglobin contains a histidine group attached directly to the iron center, and a distal histidine group on the opposite face, not bonded to the iron.

Many functional models of myoglobin have been studied. One of the most important are that of picket fence porphyrin by James Collman. This model was used to show the importance of the distal prosthetic group. It serves three functions:

  1. to form hydrogen bonds with the dioxygen moiety, increasing the O2 binding constant
  2. to prevent the binding of hemoglobin and myoglobin. Oxygen binds in a bent fashion, which can fit with the distal histidine.[11]
  3. to prevent irreversible dimerization of the oxymyoglobin with another deoxymyoglobin species

See also

References

  1. ^ Takano, T. "Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale". J. Mol. Biol. 110: 569-584.
  2. ^ George A. Ordway and Daniel J. Garry (2004). "Myoglobin: an essential hemoprotein in striated muscle". Journal of Experimental Biology 207: pages 3441–3446. doi:10.1242/jeb.01172.
  3. ^ Harvey Lodish, Arnold Berk, Lawrence S. Zipursky, Paul Matsudaira, David Baltimore and James Darnell (2000). "Evolutionary tree showing the globin protein family members myoglobin and hemoglobin", Molecular Cell Biology, Fourth Edition, W. H. FREEMAN. ISBN 0-7167-3136-3. 
  4. ^ JC Kendrew, G Bodo, HM Dintzis, RG Parrish, H Wyckoff, and DC Phillips (1958). "A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis". Nature 181 (4610): pages 662-666. doi:10.1038/181662a0 PMID 13517261.
  5. ^ The Nobel Prize in Chemistry 1962
  6. ^ McGee, H: "On Food and Cooking: The Science and Lore of the Kitchen, page 148. Scribner: New York, 2004. ISBN 0-684-80001-2
  7. ^ Minneapolis Star Tribune, Nov. 14, 2007 http://www.startribune.com/10223/story/1548852.html
  8. ^ Minneapolis Star Tribune, October 31, 2007 http://www.startribune.com/535/story/1518775.html
  9. ^ Toshio Naka, Daryl Jones, Ian Baldwin, Nigel Fealy, Samantha Bates, Hermann Goehl, Stanislao Morgera, Hans H. Neumayer and Rinaldo Bellomo (2005). "Myoglobin clearance by super high-flux hemofiltration in a case of severe rhabdomyolysis: a case report". Critical Care 9: pages R90–R95. doi:10.1186/cc3034.
  10. ^ M. Weber, M. Rau, K. Madlener, A. Elsaesser, D. Bankovic, V. Mitrovic and C. Hamm (2005). "Diagnostic utility of new immunoassays for the cardiac markers cTnI, myoglobin and CK-MB mass". Clinical Biochemistry 38: pages 1027–1030. Entrez PubMed 16125162.
  11. ^ J. P. Collman, J. I. Brauman, T. R. Halbert, and K. S. Suslick (1976). "Nature of Oxygen and Carbon Monoxide Binding to Metalloporphyrins and Heme Proteins". Proceedings of the National Academy of Sciences of the United States of America 73 (10): 3333-3337.

Further reading

  • J. P. Collman, R. Boulatov, C. J. Sunderland and L. Fu (2004). "Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin". Chem. Rev. 104 (2): 561-588. doi:10.1021/cr0206059.
  • Reeder, BJ; Svistunenko DA, Cooper CE, Wilson MT (Dec 2004). "The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology". Antioxid Redox Signal 6 (6): 954-66. PMID 15548893.
  • Schlieper, G; Kim JH, Molojavyi A, Jacoby C, Laussmann T, Flogel U, Godecke A, Schrader J (Apr 2004). "Adaptation of the myoglobin knockout mouse to hypoxic stress". Am J Physiol Regul Integr Comp Physiol 286 (4): R786-92. PMID 14656764.
  • Takano, T. "Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale". J. Mol. Biol. 110: 569-584.
  • Roy, A; Sen S, Chakraborti AS (Feb 2004). "In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress". Free Radic Res. 38 (2): 139-46. PMID 15104207.
  • Stewart, JM; Blakely JA, Karpowicz PA, Kalanxhi E, Thatcher BJ, Martin BM (Mar 2004). "Unusually weak oxygen binding, physical properties, partial sequence, autoxidation rate and a potential phosphorylation site of beluga whale (Delphinapterus leucas) myoglobin". Comp Biochem Physiol B Biochem Mol Biol 137 (3): 401-12. PMID 15050527.
  • Wu, G; Wainwright LM, Poole RK (2003). "Microbial globins". Adv Microb Physiol 47: 255-310. PMID 14560666.
 
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