Myoglobin

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Myoglobin

Myoglobin (/maɪˈoʊɡloʊbɪn/; from Greek: μυς myo, "muscle" + γλόβος globus, "sphere") 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.

Etymology

The term "myoglobin" is derived from the Greek words "myo", meaning muscle, and "globin", meaning sphere. This is in reference to the protein's role in muscle oxygen storage and its globular structure.

Function

Myoglobin's primary function is to store oxygen in muscle cells, which it accomplishes due to its heme (iron-containing porphyrin) group. Myoglobin receives oxygen from hemoglobin in the bloodstream and then stores it until the muscle requires oxygen for energy production.

Structure

Myoglobin is a single-chain polypeptide consisting of 153 amino acids. It contains a heme (prosthetic) group in the center around which the remaining apoprotein folds. It is a globular protein that is water soluble.

Related Terms

  • Hemoglobin: The protein in red blood cells that carries oxygen from the lungs to the body's tissues and returns carbon dioxide from the tissues back to the lungs.
  • Heme: An iron-containing compound of the porphyrin class that forms the nonprotein part of hemoglobin and some other biological molecules.
  • Porphyrin: Any of a class of heterocyclic compounds that are widely distributed in nature and include many biological pigments, such as chlorophyll and hemoglobin.

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