Myoglobin
Structure = molecular structure | Review = role in human pathologies,
gene knockout | Diseases= kidney disease, vasospasm}}
protozoan/eubacterial? | Cells = muscle cells | Location = cytoplasm }}
phosphorylation in whales? | Names = myoglobin-like proteins in microorganisms | Interactions = oxygen,
heme,
carbon monoxide,
nitric oxide | Pages = X-ray crystallography,
Secondary structure}}
Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. With a molecular weight of 16,700 Daltons, it is the primary oxygen-carrying pigment of muscle tissues[ }}]. Unlike the blood-borne hemoglobin, to which it is structurally related[Oxy-myoglobin at 0.1 nm resolution: PDB 1A6M. Sperm whale myoglobin at 0.17 nm resolution: PDB 1VXH.].For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz[The Nobel Prize in Chemistry 1962].Myoglobin has been implicated as a cause of acute renal failure following damage to muscle tissue (e.g. rhabdomyolysis, severe crush trauma, malignant hyperthermia, status epilepticus and neuroleptic malignant syndrome), due to its toxicity to renal tubular epithelium[ }}].
Myoglobin is a sensitive marker for muscle injury, making it a potential marker for myocardial infarction in patients with chest pain[}}]. Its specificity and the cost of the analysis has prevented its widespread use.
During muscle death due to infarction, myoglobin is released, which is toxic to the kidneys. If it is misdiagnosed, it can cause much worse conditions, such as cardiac arrest.
* hemoglobin
* hemoprotein*Protein Database featured molecule
* human genetics
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