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Function

Mechanism

The structure of this protein comprises of two prominent domains. The larger one contains an N terminal distorted beta-barrel accompanied by alpha helices. The second and smaller unit is consist of a beta sheet and alpha helix complex (Viviani, 2002). The process of fluorescence is achieved through a two-step oxidation reaction involving the substrate Lucinferin accompanied with ATP, Magnesium and oxygen. The first step consist of using ATP-Mg in an Acylation reaction of the COOH group on Lucinferin producing a Luciferyl adenylate intermediate and a phosphate group. The second reaction uses oxygen to create an excited state of the molecule. The molecule then returns to its ground state emitting a photon of light (Conti et al., 1996). A single peptide has been discover that plays a vital role in the photooxidation by Luciferase. The specific amino acid is a histidine located in the region 244HHGF247 of the protein (Branchini, 1997). It has been shown to be necessary for the use of oxygen in the second part of the reaction.

Disease

Relevance

Structural highlights

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