Myoglobin - wikipedia Myoglobin MB Available structures PDB Ortholog search : PDBe RCSB List of PDB id codes 3RGK Identifiers Aliases MB, PVALB, myoglobgin, myoglobin, Myoglobin External IDs OMIM : 160000 MGI : 96922 HomoloGene : 3916 GeneCards : MB Gene location ( Human ) Chr. Chromosome 22 ( human ) Band 22q12. 3 Start 35,606,764 bp End 35,637,951 bp Gene location ( Mouse ) Chr. Chromosome 15 ( mouse ) Band 15 D3 15 36.36 cM Start 77,015,489 bp End 77,050,670 bp RNA expression pattern More reference expression data Gene ontology Molecular function oxygen binding heme binding metal ion binding oxygen transporter activity Cellular component extracellular exosome cytosol Biological process response to hormone heart development slow - twitch skeletal muscle fiber contraction response to hypoxia enucleate erythrocyte differentiation response to hydrogen peroxide brown fat cell differentiation oxygen transport transport Sources : Amigo / QuickGO Orthologs Species Human Mouse Entrez 4151 17189 Ensembl ENSG00000198125 ENSMUSG00000018893 UniProt P02144 P04247 RefSeq ( mRNA ) NM_005368 NM_203377 NM_203378 NM_001362846 NM_001164047 NM_001164048 NM_013593 RefSeq ( protein ) NP_005359 NP_976311 NP_976312 NP_001349775 NP_001157519 NP_001157520 NP_038621 Location ( UCSC ) Chr 22 : 35.61 -- 35.64 Mb Chr 15 : 77.02 -- 77.05 Mb PubMed search Wikidata View / Edit Human View / Edit Mouse Myoglobin ( symbol Mb or MB ) is an iron - and oxygen - binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron - and oxygen - binding protein in blood, specifically in the red blood cells. In humans, myoglobin is only found in the bloodstream after muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood. Myoglobin is the primary oxygen - carrying pigment of muscle tissues. High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A and Type II B, but most texts consider myoglobin not to be found in smooth muscle. Myoglobin was the first protein to have its three - dimensional structure revealed by X-ray crystallography. This achievement was reported in 1958 by John Kendrew and associates. For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz. Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established : mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin - deplete mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, oxygen storage and as a scavenger of reactive oxygen species. In humans myoglobin is encoded by the MB gene. Hemoglobin can take the forms of oxyhemoglobin ( HbO ), carboxyhemoglobin ( HbCO ), and methemoglobin ( met - Hb ) ; similarly, myoglobin can take the forms of oxymyoglobin ( MbO ), carboxymyoglobin ( MbCO ), and metmyoglobin ( met - Mb ). Contents 1 Differences from hemoglobin 2 Meat color 3 Role in disease 4 Structure and bonding 5 Synthetic analogues 6 See also 7 References 8 Further reading 9 External links Differences from hemoglobin Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one heme group, whereas hemoglobin has four. Although its heme group is identical to those in Hb, Mb has a higher affinity for oxygen than does hemoglobin. This difference is related to its different role : whereas hemoglobin transports oxygen, myoglobin 's function is to store oxygen. Meat color Myoglobin contains hemes, pigments responsible for the colour of red meat. The colour that meat takes is partly determined by the degree of oxidation of the myoglobin. In fresh meat the iron atom is in the ferrous ( + 2 ) oxidation state bound to an oxygen molecule ( O ). Meat cooked well done is brown because the iron atom is now in the ferric ( + 3 ) oxidation state, having lost an electron. If meat has been exposed to nitrites, it will remain pink because the iron atom is bound to NO, 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 to a molecule of carbon monoxide. Raw meat packed in a carbon monoxide atmosphere also shows this same pink `` smoke ring '' due to the same principles. Notably, the surface of this raw meat also displays the pink color, which is usually associated in consumers ' minds with fresh meat. This artificially induced pink color can persist, reportedly up to one year. 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. 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 kidney injury. It is not the myoglobin itself that is toxic ( it is a protoxin ) but the ferrihemate portion that is dissociated from myoglobin in acidic environments ( e.g., acidic urine, lysosomes ). Myoglobin is a sensitive marker for muscle injury, making it a potential marker for heart attack in patients with chest pain. However, elevated myoglobin has low specificity for acute myocardial infarction ( AMI ) and thus CK - MB, cardiac Troponin, ECG, and clinical signs should be taken into account to make the diagnosis. Structure and bonding Molecular orbital description of Fe - O interaction in myoglobin. Myoglobin belongs to the globin superfamily of proteins, and as with other globins, consists of eight alpha helices connected by loops. Hemoglobin contains 154 amino acids. Myoglobin contains a porphyrin ring with an iron at its center. A proximal histidine group ( His - 93 ) is attached directly to iron, and a distal histidine group ( His - 64 ) hovers near the opposite face. The distal imidazole is not bonded to the iron but is available to interact with the substrate O. This interaction encourages the binding of O, but not carbon monoxide ( CO ), which still binds about 240 × more strongly than O. The binding of O causes substantial structural change at the Fe center, which shrinks in radius and moves into the center of N4 pocket. O - binding induces `` spin - pairing '' : the five - coordinate ferrous deoxy form is high spin and the six coordinate oxy form is low spin and diamagnetic. This is an image of an oxygenated myoglobin molecule. The image shows the structural change when oxygen is bound to the iron atom of the heme prosthetic group. The oxygen atoms are colored in green, the iron atom is colored in red, and the heme group is colored in blue. Synthetic analogues Many models of myoglobin have been synthesized as part of a broad interest in transition metal dioxygen complexes. A well known example is the picket fence porphyrin, which consists of a ferrous complex of a sterically bulky derivative of tetraphenylporphyrin. In the presence of an imidazole ligand, this ferrous complex reversibly binds O. The O substrate adopts a bent geometry, occupying the sixth position of the iron center. A key property of this model is the slow formation of the μ - oxo dimer, which is an inactive diferric state. In nature, such deactivation pathways are suppressed by protein matrix that prevents close approach of the Fe - porphyrin assemblies. A picket - fence porphyrin complex of Fe, with axial coordination sites occupied by methylimidazole ( green ) and dioxygen. The R groups flank the O - binding site. See also Cytoglobin Hemoglobin Hemoprotein Neuroglobin Phytoglobin Myoglobinuria - The presence of myoglobin in the urine Ischemia - reperfusion injury of the appendicular musculoskeletal system References ^ Jump up to : GRCh38 : Ensembl release 89 : ENSG00000198125 - Ensembl, May 2017 ^ Jump up to : GRCm38 : Ensembl release 89 : ENSMUSG00000018893 - Ensembl, May 2017 Jump up ^ `` Human PubMed Reference : ''. Jump up ^ `` Mouse PubMed Reference : ''. ^ Jump up to : Nelson DL, Cox MM ( 2000 ). Lehninger Principles of Biochemistry ( 3rd ed. ). New York : Worth Publishers. p. 206. ISBN 0 - 7167 - 6203 - X. ( Google books link is the 2008 edition ) Jump up ^ Ordway GA, Garry DJ ( Sep 2004 ). `` Myoglobin : an essential hemoprotein in striated muscle ''. The Journal of Experimental Biology. 207 ( Pt 20 ) : 3441 -- 6. doi : 10.1242 / jeb. 01172. PMID 15339940. Jump up ^ ( U.S. ) National Science Foundation : Protein Data Bank Chronology ( Jan. 21, 2004 ). Retrieved 3.17. 2010 Jump up ^ Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC ( Mar 1958 ). `` A three - dimensional model of the myoglobin molecule obtained by x-ray analysis ''. Nature. 181 ( 4610 ) : 662 -- 6. Bibcode : 1958Natur. 181... 662K. doi : 10.1038 / 181662a0. PMID 13517261. Jump up ^ The Nobel Prize in Chemistry 1962 Jump up ^ Garry DJ, Kanatous SB, Mammen PP ( 2007 ). `` Molecular insights into the functional role of myoglobin ''. Advances in Experimental Medicine and Biology. 618 : 181 -- 93. doi : 10.1007 / 978 - 0 - 387 - 75434 - 5_14. PMID 18269197. Jump up ^ Akaboshi E ( 1985 ). `` Cloning of the human myoglobin gene ''. Gene. 33 ( 3 ) : 241 -- 9. doi : 10.1016 / 0378 - 1119 ( 85 ) 90231 - 8. PMID 2989088. Jump up ^ McGee H ( 2004 ). On Food and Cooking : The Science and Lore of the Kitchen. New York : Scribner. p. 148. ISBN 0 - 684 - 80001 - 2. Jump up ^ Fraqueza MJ, Barreto AS ( Sep 2011 ). `` Gas mixtures approach to improve turkey meat shelf life under modified atmosphere packaging : the effect of carbon monoxide ''. Poultry Science. 90 ( 9 ) : 2076 -- 84. doi : 10.3382 / ps. 2011 - 01366. PMID 21844276. Jump up ^ Associated Press ( 2007 - 10 - 30 ). `` Meat companies defend use of carbon monoxide ''. Business. Minneapolis Star Tribune. Jump up ^ Naka T, Jones D, Baldwin I, Fealy N, Bates S, Goehl H, Morgera S, Neumayer HH, Bellomo R ( Apr 2005 ). `` Myoglobin clearance by super high - flux hemofiltration in a case of severe rhabdomyolysis : a case report ''. Critical Care. 9 ( 2 ) : R90 -- 5. doi : 10.1186 / cc3034. PMC 1175920. PMID 15774055. Jump up ^ Weber M, Rau M, Madlener K, Elsaesser A, Bankovic D, Mitrovic V, Hamm C ( Nov 2005 ). `` Diagnostic utility of new immunoassays for the cardiac markers cTnI, myoglobin and CK - MB mass ''. Clinical Biochemistry. 38 ( 11 ) : 1027 -- 30. doi : 10.1016 / j. clinbiochem. 2005.07. 011. PMID 16125162. Jump up ^ Drago RS ( 1980 ). `` Free radical reactions of transition metal systems ''. Coordination Chemistry Reviews. 32 ( 2 ) : 97 -- 110. doi : 10.1016 / S0010 - 8545 ( 00 ) 80372 - 0. ^ Jump up to : Universal protein resource accession number P02144 at UniProt. Jump up ^ Collman JP, Brauman JI, Halbert TR, Suslick KS ( Oct 1976 ). `` Nature of O2 and CO binding to metalloporphyrins and heme proteins ''. Proceedings of the National Academy of Sciences of the United States of America. 73 ( 10 ) : 3333 -- 7. Bibcode : 1976PNAS... 73.3333 C. doi : 10.1073 / pnas. 73.10. 3333. PMC 431107. PMID 1068445. Jump up ^ Lippard SJ, Berg JM ( 1994 ). Principles of Bioinorganic Chemistry. Mill Valley, CA : University Science Books. ISBN 0 - 935702 - 73 - 3. Further reading Collman JP, Boulatov R, Sunderland CJ, Fu L ( Feb 2004 ). `` Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin ''. Chemical Reviews. 104 ( 2 ) : 561 -- 88. doi : 10.1021 / cr0206059. PMID 14871135. 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 ''. Antioxidants & Redox Signaling. 6 ( 6 ) : 954 -- 66. doi : 10.1089 / ars. 2004.6. 954. PMID 15548893. Schlieper G, Kim JH, Molojavyi A, Jacoby C, Laussmann T, Flögel U, Gödecke A, Schrader J ( Apr 2004 ). `` Adaptation of the myoglobin knockout mouse to hypoxic stress ''. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. 286 ( 4 ) : R786 -- 92. doi : 10.1152 / ajpregu. 00043.2003. PMID 14656764. Takano T ( Mar 1977 ). `` Structure of myoglobin refined at 2 - 0 A resolution. II. Structure of deoxymyoglobin from sperm whale ''. Journal of Molecular Biology. 110 ( 3 ) : 569 -- 84. doi : 10.1016 / S0022 - 2836 ( 77 ) 80112 - 5. PMID 845960. Roy A, Sen S, Chakraborti AS ( Feb 2004 ). `` In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress ''. Free Radical Research. 38 ( 2 ) : 139 -- 46. doi : 10.1080 / 10715160310001638038. 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 ''. Comparative Biochemistry and Physiology B. 137 ( 3 ) : 401 -- 12. doi : 10.1016 / j. cbpc. 2004.01. 007. PMID 15050527. Wu G, Wainwright LM, Poole RK ( 2003 ). `` Microbial globins ''. Advances in Microbial Physiology. Advances in Microbial Physiology. 47 : 255 -- 310. doi : 10.1016 / S0065 - 2911 ( 03 ) 47005 - 7. ISBN 9780120277476. PMID 14560666. Mirceta S, Signore AV, Burns JM, Cossins AR, Campbell KL, Berenbrink M ( Jun 2013 ). `` Evolution of mammalian diving capacity traced by myoglobin net surface charge ''. Science. 340 ( 6138 ) : 1234192. doi : 10.1126 / science. 1234192. PMID 23766330... Also see Proteopedia article about this finding External links Online Mendelian Inheritance in Man ( OMIM ) 160000 human genetics The Myoglobin Protein Protein Database featured molecule Which Cut Is Older ? ( It 's a Trick Question ) New York Times, February 21, 2006 article regarding meat industry use of carbon monoxide to keep meat looking red. Stores React to Meat Reports New York Times, March 1, 2006 article on the use of carbon monoxide to make meat appear fresh. PDB gallery 1m6c : V68N MYOGLOBIN WITH CO 1m6m : V68N MET MYOGLOBIN 1mdn : WILD TYPE MYOGLOBIN WITH CO 1mnh : INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS : ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN 1mni : ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS - IMIDAZOLE LIGATION IN THE HIS64 -- > VAL ( SLASH ) VAL68 -- > HIS DOUBLE MUTANT 1mnj : INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS : ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN 1mnk : INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS : ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN 1mno : V68N MYOGLOBIN OXY FORM 1mwc : WILD TYPE MYOGLOBIN WITH CO 1mwd : WILD TYPE DEOXY MYOGLOBIN 1myg : HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB ( LYS45 - > ARG ) AND MB ( LYS45 - > SER ) 1myh : HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB ( LYS45 - > ARG ) AND MB ( LYS45 - > SER ) 1myi : HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB ( LYS45 - > ARG ) AND MB ( LYS45 - > SER ) 1myj : DISTAL POLARITY IN LIGAND BINDING TO MYOGLOBIN : STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A THREONINE68 ( E11 ) MUTANT 1pmb : THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT 1yca : DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN : DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 ( E11 ) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY 1ycb : DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN : DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 ( E11 ) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY 2mm1 : X-RAY CRYSTAL STRUCTURE OF A RECOMBINANT HUMAN MYOGLOBIN MUTANT AT 2.8 ANGSTROMS RESOLUTION Proteins : hemeproteins Globins Hemoglobin Subunits Alpha locus on 16 : α HBA1 HBA2 ζ HBZ θ HBQ1 μ HBM Beta locus on 11 : β HBB δ HBD γ HBG1 HBG2 ε HBE1 Tetramers stages of development : Embryonic HbE Gower 1 ( ζ ε ) HbE Gower 2 ( α ε ) HbE Portland I ( ζ γ ) HbE Portland II ( ζ β ) Fetal HbF / Fetal ( α γ ) HbA ( α β ) Adult HbA ( α β ) HbA ( α δ ) HbF / Fetal ( α γ ) pathology : HbH ( β ) Barts ( γ ) HbS ( α β ) HbC ( α β ) HbE ( α β ) Compounds Carboxyhemoglobin Carbaminohemoglobin Oxyhemoglobin / Deoxyhemoglobin Sulfhemoglobin Other human Glycated hemoglobin Methemoglobin Nonhuman Chlorocruorin Erythrocruorin Other human : Myoglobin Metmyoglobin Neuroglobin Cytoglobin plant : Leghemoglobin Other Cytochrome Cytochrome b Cytochrome P450 Hemocyanin Methemalbumin see also disorders of globin and globulin proteins Common for blood tests ( CPT 82000 -- 84999 ) Electrolytes Sodium Potassium Chloride Calcium Renal function Creatinine Urea BUN - to - creatinine ratio Plasma osmolality Serum osmolal gap Acid - base Anion gap Arterial blood gas Base excess Bicarbonate CO content Iron tests Ferritin Serum iron Transferrin saturation Total iron - binding capacity Transferrin Transferrin receptor Hormones ACTH stimulation test Thyroid function tests Thyroid - stimulating hormone Metabolism Blood lipids Cardiovascular Cardiac marker Troponin test CPK - MB test Lactate dehydrogenase Myoglobin Glycogen phosphorylase isoenzyme BB Liver function tests Proteins Human serum albumin Serum total protein ALP transaminases ALT AST AST / ALT ratio Bilirubin Unconjugated Conjugated Pancreas Amylase Lipase Pancreatic lipase NDL : 00567709 Retrieved from `` https://en.wikipedia.org/w/index.php?title=Myoglobin&oldid=843344585 '' Categories : Genes on human chromosome 22 Hemoproteins Human proteins Hidden categories : All articles with unsourced statements Articles with unsourced statements from March 2017 Talk Contents About Wikipedia বাংলা Български Bosanski Català Čeština Dansk Deutsch Ελληνικά Español Esperanto Euskara فارسی Français Galego Հայերեն Bahasa Indonesia Italiano עברית Қазақша Кыргызча Lietuvių Magyar Nederlands 日本 語 Norsk Polski Português Română Русский Scots Simple English Slovenščina Српски / srpski Srpskohrvatski / српскохрватски Suomi Svenska ไทย Türkçe Українська 粵語 中文 33 more Edit links This page was last edited on 28 May 2018, at 14 : 47. 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Question: a protein found in muscle that can bind to and store oxygen
Answer: Myoglobin