Myoglobin

Last updated
MB
ChimeraX rendering of myoglobin (PDB 2SPL).png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MB , PVALB, myoglobgin, myoglobin, Myoglobin
External IDs OMIM: 160000; MGI: 96922; HomoloGene: 3916; GeneCards: MB; OMA:MB - orthologs
Orthologs
SpeciesHumanMouse
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_001157519
NP_001157520
NP_038621

Location (UCSC) Chr 22: 35.61 – 35.64 Mb Chr 15: 76.9 – 76.93 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. [5] [6] [7] [8] [9] Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. [8] [10] Myoglobin consists of non-polar amino acids at the core of the globulin, where the heme group is non-covalently bounded with the surrounding polypeptide of myoglobin. In humans, myoglobin is found in the bloodstream only after muscle injury. [11] [12] [13]

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. [13] Myoglobin is found in Type I muscle, Type II A, and Type II B; although many older texts describe myoglobin as not found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells. [14]

Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography. [15] This achievement was reported in 1958 by John Kendrew and associates. [16] For this discovery, Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz. [17] [18] 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-depleted mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, and to oxygen storage; as well, it serves as a scavenger of reactive oxygen species. [19]

In humans, myoglobin is encoded by the MB gene. [20]

Myoglobin can take the forms oxymyoglobin (MbO2), carboxymyoglobin (MbCO), and metmyoglobin (met-Mb), analogously to hemoglobin taking the forms oxyhemoglobin (HbO2), carboxyhemoglobin (HbCO), and methemoglobin (met-Hb). [21]

Differences from hemoglobin

Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one globulin 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 but fewer total oxygen-storage capacities. [22] The newest discovery reveals that myoglobin facilitates oxygen diffusion down a gradient, enhancing oxygen transport in mitochondria.[ citation needed ]

Role in cuisine

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 (O2). 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 reddish pink "smoke ring" that comes from the heme center binding to carbon monoxide. [23] 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. [24] Hormel and Cargill (meat processing companies in the US) are both reported to use this meat-packing process, and meat treated this way has been in the consumer market since 2003. [25]

Meat alternatives have used various ways to recreate the "meaty" taste associated with myoglobin. Impossible Foods uses leghemoglobin, a heme-containing globin from soy root nodule, produced as a recombinant protein in Komagataella ("Pichia pastoris") yeast. [26] [27] Motif FoodWorks produces a recombinant bovine myoglobin using Komagataella yeast, [28] considered GRAS by the FDA. [29] Moolec Science has engineered a soybean that produces porcine myoglobin in its seeds called "Piggy Sooy"; it was approved by the USDA in April 2024. [30]

Role in disease

Myoglobin is released from damaged muscle tissue, which contain very high concentrations of myoglobin. [31] The released myoglobin enters the bloodstream, where high levels may indicate rhabdomyolysis. The myoglobin is filtered by the kidneys, but is toxic to the renal tubular epithelium and so may cause acute kidney injury. [32] 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).[ citation needed ]

Myoglobin is a sensitive marker for muscle injury, making it a potential marker for heart attack in patients with chest pain. [33] 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. [34]

Structure and bonding

Myoglobin belongs to the globin superfamily of proteins, and as with other globins, consists of eight alpha helices connected by loops. Myoglobin contains 153 amino acids. [35]

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. [35] The distal imidazole is not bonded to the iron, but is available to interact with the substrate O2. This interaction encourages the binding of O2, but not carbon monoxide (CO), which still binds about 240× more strongly than O2.[ citation needed ]

The binding of O2 causes substantial structural change at the Fe center, which shrinks in radius and moves into the center of N4 pocket. O2-binding induces "spin-pairing": the five-coordinate ferrous deoxy form is high spin and the six coordinate oxy form is low spin and diamagnetic.[ citation needed ]

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. [37] In the presence of an imidazole ligand, this ferrous complex reversibly binds O2. The O2 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. [38]

A picket-fence porphyrin complex of Fe, with axial coordination sites occupied by methylimidazole (green) and dioxygen. The R groups flank the O2-binding site. PicketFenceGenericRevised.png
A picket-fence porphyrin complex of Fe, with axial coordination sites occupied by methylimidazole (green) and dioxygen. The R groups flank the O2-binding site.

See also

Related Research Articles

<span class="mw-page-title-main">Hemoglobin</span> Metalloprotein that binds with oxygen

Hemoglobin is a protein containing iron that facilitates the transport of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, with the exception of the fish family Channichthyidae. Hemoglobin in the blood carries oxygen from the respiratory organs to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers the animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and globulin.

<span class="mw-page-title-main">Red blood cell</span> Oxygen-delivering blood cell and the most common type of blood cell

Red blood cells (RBCs), scientific name erythrocytes (from ancient Greek erythros 'red' and kytos 'hollow vessel', with -cyte translated as 'cell' in modern usage), also known as red cells, erythroid cells, and rarely haematids, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen (O2) to the body tissues—via blood flow through the circulatory system. Erythrocytes take up oxygen in the lungs, or in fish the gills, and release it into tissues while squeezing through the body's capillaries.

<span class="mw-page-title-main">Hemoprotein</span> Protein containing a heme prosthetic group

A hemeprotein, or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.

<span class="mw-page-title-main">Leghemoglobin</span> Oxygen-carrying phytoglobin found in rhizome of leguminous plants

Leghemoglobin is an oxygen-carrying phytoglobin found in the nitrogen-fixing root nodules of leguminous plants. It is produced by these plants in response to the roots being colonized by nitrogen-fixing bacteria, termed rhizobia, as part of the symbiotic interaction between plant and bacterium: roots not colonized by Rhizobium do not synthesise leghemoglobin. Leghemoglobin has close chemical and structural similarities to hemoglobin, and, like hemoglobin, is red in colour. It was originally thought that the heme prosthetic group for plant leghemoglobin was provided by the bacterial symbiont within symbiotic root nodules. However, subsequent work shows that the plant host strongly expresses heme biosynthesis genes within nodules, and that activation of those genes correlates with leghemoglobin gene expression in developing nodules.

<span class="mw-page-title-main">Heme</span> Chemical coordination complex of an iron ion chelated to a porphyrin

Heme, or haem, is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver.

<span class="mw-page-title-main">Hemerythrin</span> InterPro Family

Hemerythrin (also spelled haemerythrin; Ancient Greek: αἷμα, romanized: haîma, lit. 'blood', Ancient Greek: ἐρυθρός, romanized: erythrós, lit. 'red') is an oligomeric protein responsible for oxygen (O2) transport in the marine invertebrate phyla of sipunculids, priapulids, brachiopods, and in a single annelid worm genus, Magelona. Myohemerythrin is a monomeric O2-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state.

<span class="mw-page-title-main">Globin</span> Superfamily of oxygen-transporting globular proteins

The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group. They are widely distributed in many organisms.

<span class="mw-page-title-main">Carbon monoxide poisoning</span> Toxic effects of carbon monoxide

Carbon monoxide poisoning typically occurs from breathing in carbon monoxide (CO) at excessive levels. Symptoms are often described as "flu-like" and commonly include headache, dizziness, weakness, vomiting, chest pain, and confusion. Large exposures can result in loss of consciousness, arrhythmias, seizures, or death. The classically described "cherry red skin" rarely occurs. Long-term complications may include chronic fatigue, trouble with memory, and movement problems.

<span class="mw-page-title-main">Binding site</span> Molecule-specific coordinate bonding area in biological systems

In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. The binding partner of the macromolecule is often referred to as a ligand. Ligands may include other proteins, enzyme substrates, second messengers, hormones, or allosteric modulators. The binding event is often, but not always, accompanied by a conformational change that alters the protein's function. Binding to protein binding sites is most often reversible, but can also be covalent reversible or irreversible.

<span class="mw-page-title-main">Bohr effect</span> Concept in physiology

The Bohr effect is a phenomenon first described in 1904 by the Danish physiologist Christian Bohr. Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment. Since carbon dioxide reacts with water to form carbonic acid, an increase in CO2 results in a decrease in blood pH, resulting in hemoglobin proteins releasing their load of oxygen. Conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen.

<span class="mw-page-title-main">Channichthyidae</span> Family of fishes

The crocodile icefish or white-blooded fish comprise a family (Channichthyidae) of notothenioid fish found in the Southern Ocean around Antarctica. They are the only known vertebrates to lack hemoglobin in their blood as adults. Icefish populations are known to reside in the Atlantic and Indian sectors of the Southern Ocean, as well as the continental shelf waters surrounding Antarctica. Water temperatures in these regions remain relatively stable, generally ranging from −1.8 to 2 °C. One icefish, Champsocephalus esox, is distributed north of the Antarctic Polar Frontal Zone. At least 16 species of crocodile icefish are currently recognized, although eight additional species have been proposed for the icefish genus Channichthys.

Carboxyhemoglobin is a stable complex of carbon monoxide and hemoglobin (Hb) that forms in red blood cells upon contact with carbon monoxide. Carboxyhemoglobin is often mistaken for the compound formed by the combination of carbon dioxide (carboxyl) and hemoglobin, which is actually carbaminohemoglobin. Carboxyhemoglobin terminology emerged when carbon monoxide was known by its historic name, "carbonic oxide", and evolved through Germanic and British English etymological influences; the preferred IUPAC nomenclature is carbonylhemoglobin.

A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O2 transport. Other functions performed include O2 storage, CO2 transport, and transportation of substances other than respiratory gases. There are four major classifications of respiratory pigment: hemoglobin, hemocyanin, erythrocruorin–chlorocruorin, and hemerythrin. The heme-containing globin is the most commonly-occurring respiratory pigment, occurring in at least 9 different phyla of animals.

<span class="mw-page-title-main">Heme oxygenase</span> Class of enzymes

Heme oxygenase, or haem oxygenase, is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous iron, and carbon monoxide.

Iron-binding proteins are carrier proteins and metalloproteins that are important in iron metabolism and the immune response. Iron is required for life.

<span class="mw-page-title-main">Neuroglobin</span>

Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues. Neuroglobin is a monomer that reversibly binds oxygen with an affinity higher than that of hemoglobin. It also increases oxygen availability to brain tissue and provides protection under hypoxic or ischemic conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated protostomes, like photosynthetic acoel as well as radiata such as jellyfish. In addition to neurons, neuroglobin is present in astrocytes in certain pathologies of the rodent brain and in the physiological seal brain. This is thought to be due to convergent evolution. It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Recent research confirmed the presence of human neuroglobin protein in cerebrospinal fluid (CSF).

<span class="mw-page-title-main">Heme B</span> Chemical compound

Heme B or haem B is the most abundant heme. Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes (cyclooxygenase) of recent fame, also contain heme B at one of two active sites.

<span class="mw-page-title-main">Iron in biology</span> Use of Iron by organisms

Iron is an important biological element. It is used in both the ubiquitous iron-sulfur proteins and in vertebrates it is used in hemoglobin which is essential for blood and oxygen transport.

<span class="mw-page-title-main">Nitric oxide dioxygenase</span>

Nitric oxide dioxygenase (EC 1.14.12.17) is an enzyme that catalyzes the conversion of nitric oxide (NO) to nitrate (NO−
3) . The net reaction for the reaction catalyzed by nitric oxide dioxygenase is shown below:

<span class="mw-page-title-main">Carbon monoxide-releasing molecules</span> Substances delivering CO within the body

Carbon monoxide-releasing molecules (CORMs) are chemical compounds designed to release controlled amounts of carbon monoxide (CO). CORMs are being developed as potential therapeutic agents to locally deliver CO to cells and tissues, thus overcoming limitations of CO gas inhalation protocols.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000198125 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000018893 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ 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.
  6. ↑ Wick MR, Hornick JL (2011). "Immunohistology of Soft Tissue and Osseous Neoplasms". Diagnostic Immunohistochemistry. Elsevier. pp. 83–136. doi:10.1016/b978-1-4160-5766-6.00008-x. ISBN   978-1-4160-5766-6. Myoglobin is a 17.8-kD protein that is found in cardiac and skeletal muscle and that forms complexes with iron molecules.
  7. ↑ Feher J (2017). "Oxygen and Carbon Dioxide Transport". Quantitative Human Physiology. Elsevier. pp. 656–664. doi:10.1016/b978-0-12-800883-6.00064-1. ISBN   978-0-12-800883-6. Highly oxidative muscle fibers contain a lot of myoglobin. It has two functions in muscle: it stores oxygen for use during heavy exercise, and it enhances diffusion through the cytosol by carrying the oxygen. By binding O2, myoglobin (Mb) provides a second diffusive pathway for O2 through the cell cytosol.
  8. 1 2 Wilson MT, Reeder BJ (2006). "MYOGLOBIN". Encyclopedia of Respiratory Medicine. Elsevier. pp. 73–76. doi:10.1016/b0-12-370879-6/00250-7. ISBN   978-0-12-370879-3. Myoglobin (Mb) is a heme-containing globular protein that is found in abundance in myocyte cells of heart and skeletal muscle.
  9. ↑ Boncyk JC (2007). "Perioperative Hypoxia". Complications in Anesthesia. Elsevier. pp. 193–199. doi:10.1016/b978-1-4160-2215-2.50052-1. ISBN   978-1-4160-2215-2. Myoglobin serves both as an O2 buffer and to store O2 in muscle. All known vertebrate myoglobins and β-hemoglobin subunits are similar in structure, but myoglobin binds O2 more avidly at low Po2 (Fig. 47-5) because it is a monomer (i.e., it does not undergo a significant conformational change with oxygenation). Thus, myoglobin remains fully saturated at O2 tensions between 15 and 30 mm Hg and unloads its O2 to the muscle mitochondria only at very low O2 tensions.
  10. ↑ Hardison RC (Dec 2012). "Evolution of Hemoglobin and Its Genes". Cold Spring Harb Perspect Med. 2 (12): a011627. doi:10.1101/cshperspect.a011627. PMC   3543078 . PMID   23209182.
  11. ↑ Chung MJ, Brown DL (July 2018). "Diagnosis of acute myocardial infarction.". In Brown DL (ed.). Cardiac Intensive Care-E-Book. pp. 91–98.e3. doi:10.1016/B978-0-323-52993-8.00009-6. ISBN   9780323529938. S2CID   260507329. Myoglobin is not specific for myocardial necrosis, however, especially in the presence of skeletal muscle injury and renal insufficiency.
  12. ↑ Sekhon N, Peacock WF (2019). "Biomarkers to Assist in the Evaluation of Chest Pain". Biomarkers in Cardiovascular Disease. Elsevier. pp. 115–128. doi:10.1016/b978-0-323-54835-9.00011-9. ISBN   978-0-323-54835-9. S2CID   59548142. myoglobin is not specific for the death of cardiac myocytes, and levels can be elevated in renal disease as well as damage to skeletal muscle.
  13. 1 2 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)
  14. ↑ Qiu Y, Sutton L, Riggs AF (Sep 1998). "Identification of myoglobin in human smooth muscle". Journal of Biological Chemistry. 273 (36): 23426–32. doi: 10.1074/jbc.273.36.23426 . PMID   9722578.
  15. ↑ (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004). Retrieved 3.17.2010
  16. ↑ 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. S2CID   4162786.
  17. ↑ Stoddart C (1 March 2022). "Structural biology: How proteins got their close-up". Knowable Magazine. doi: 10.1146/knowable-022822-1 . Retrieved 25 March 2022.
  18. ↑ The Nobel Prize in Chemistry 1962
  19. ↑ Garry DJ, Kanatous SB, Mammen PP (2007). "Molecular Insights into the Functional Role of Myoglobin". Hypoxia and the Circulation. Advances in Experimental Medicine and Biology. Vol. 618. Springer. pp.  181–93. doi:10.1007/978-0-387-75434-5_14. ISBN   978-0-387-75433-8. PMID   18269197.
  20. ↑ Akaboshi E (1985). "Cloning of the human myoglobin gene". Gene. 33 (3): 241–9. doi:10.1016/0378-1119(85)90231-8. PMID   2989088.
  21. ↑ Harvey JW (2008). "Iron Metabolism and Its Disorders". Clinical Biochemistry of Domestic Animals. Elsevier. pp. 259–285. doi:10.1016/b978-0-12-370491-7.00009-x. ISBN   978-0-12-370491-7. Myoglobin is an oxygen-binding protein located primarily in muscles. Myoglobin serves as a local oxygen reservoir that can temporarily provide oxygen when blood oxygen delivery is insufficient during periods of intense muscular activity. Iron within the heme group must be in the Fe+2 state to bind oxygen. If iron is oxidized to the Fe+3 state, metmyoglobin is formed.
  22. ↑ Wilson MT, Reeder BJ (2006). "Myoglobin". In Laurent GJ, Shapiro SD (eds.). Encyclopedia of Respiratory Medicine. Oxford: Academic Press. pp. 73–76. doi:10.1016/b0-12-370879-6/00250-7. ISBN   978-0-12-370879-3.
  23. ↑ McGee H (2004). On Food and Cooking: The Science and Lore of the Kitchen. New York: Scribner. p. 148. ISBN   0-684-80001-2.
  24. ↑ 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.
  25. ↑ "Meat companies defend use of carbon monoxide". Business. Minneapolis Star Tribune. Associated Press. 2007-10-30. Archived from the original on 2013-12-25. Retrieved 2013-02-11.
  26. ↑ Shelton K, Najera K, Ajredini S, Navarro J, Frangias T (April 2020). "The Molecular Magic of "Meatless" Meats: Structural and Sequence Similarities between Soy Leghemoglobin and Bovine Globins". The FASEB Journal. 34 (S1): 1. doi: 10.1096/fasebj.2020.34.s1.04866 .
  27. ↑ Bandoim L (December 20, 2019). "What The FDA's Decision About Soy Leghemoglobin Means For Impossible Burger". Forbes . Retrieved March 4, 2020.
  28. ↑ "'A gamechanger for flavor in meat alternatives...' Motif FoodWorks to launch heme-binding protein delivering 'flavor and aroma of real meat'". foodnavigator-usa.com. 17 September 2021.
  29. ↑ "Re: GRAS Notice No. GRN 001001". fda.gov. 2021-12-03.
  30. ↑ "Moolec Becomes First Molecular Farming Company to Achieve USDA Approval for Plant-Grown Animal Proteins". Yahoo Finance. 22 April 2024.
  31. ↑ Berridge BR, Van Vleet JF, Herman E (2013). "Cardiac, Vascular, and Skeletal Muscle Systems". Haschek and Rousseaux's Handbook of Toxicologic Pathology. Elsevier. pp. 1567–1665. doi:10.1016/b978-0-12-415759-0.00046-7. ISBN   978-0-12-415759-0. Myoglobin is a low molecular weight oxygen binding heme protein that is found exclusively in heart and skeletal muscle cells. In blood, myoglobin is bound primarily to plasma globulins, a complex which is filtered by the kidneys. If the plasma concentration exceeds the plasma binding capacity (1.5 mg/dl in humans), myoglobin begins to appear in the urine. High concentrations of myoglobin can change the color of the urine to a dark red-brown color.
  32. ↑ Naka T, Jones D, Baldwin I, Fealy N, Bates S, Goehl H, et al. (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.
  33. ↑ Weber M, Rau M, Madlener K, Elsaesser A, Bankovic D, Mitrovic V, et al. (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.
  34. ↑ Dasgupta A, Wahed A (2014). "Cardiac Markers". Clinical Chemistry, Immunology and Laboratory Quality Control. Elsevier. pp. 127–144. doi:10.1016/b978-0-12-407821-5.00008-5. ISBN   978-0-12-407821-5. Myoglobin is a heme protein found in both skeletal and cardiac muscle. Myoglobin is typically released in the circulation as early as 1 h after myocardial infarction,... Myoglobin has poor clinical specificity due to the presence of large quantities of myoglobin in skeletal muscle. Some studies suggest adding the myoglobin test to the troponin I test in order to improve diagnostic value [4]. Myoglobin, being a small protein, is excreted in urine, and a high level of serum myoglobin is encountered in patients with acute renal failure (uremic syndrome). Acute renal failure is also a complication of rhabdomyolysis, ...
  35. 1 2 Universal protein resource accession number P02144 at UniProt.
  36. ↑ 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.
  37. ↑ 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...73.3333C. doi: 10.1073/pnas.73.10.3333 . PMC   431107 . PMID   1068445.
  38. ↑ Lippard SJ, Berg JM (1994). Principles of Bioinorganic Chemistry. Mill Valley, CA: University Science Books. ISBN   0-935702-73-3.

Further reading

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.