Aequorin
A calcium-activated photoprotein
Aequorin is a calcium-binding protein that emits light upon binding with calcium ions. It is a bioluminescent protein originally isolated from the jellyfish Aequorea victoria. Aequorin is widely used in biochemistry and cell biology to measure calcium concentrations in biological systems.
Structure
Aequorin is composed of a single polypeptide chain that binds to a chromophore called coelenterazine. The protein has a unique structure that allows it to undergo a conformational change upon binding calcium ions, which results in the oxidation of coelenterazine and the emission of blue light. The structure of aequorin has been determined by X-ray crystallography, revealing a compact, globular shape.
Mechanism of Action
Aequorin functions as a calcium indicator by undergoing a chemical reaction in the presence of calcium ions. When calcium binds to aequorin, it triggers the oxidation of coelenterazine, leading to the production of coelenteramide, carbon dioxide, and blue light. This luminescent reaction is highly specific to calcium, making aequorin a valuable tool for measuring calcium levels in living cells.
Applications
Aequorin is used extensively in biological research to study calcium signaling pathways. It is employed in neuroscience to monitor calcium dynamics in neurons, in cardiology to study calcium's role in heart muscle contraction, and in pharmacology to screen for drugs that affect calcium channels. Aequorin's ability to provide real-time measurements of calcium concentrations makes it an essential tool in cell physiology.
History
Aequorin was first isolated in the early 1960s by Osamu Shimomura, who later received the Nobel Prize in Chemistry for his work on bioluminescence. The discovery of aequorin and its properties has significantly advanced the field of calcium imaging and has led to the development of other calcium-sensitive indicators.
Related pages
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Structure of Aequorin
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