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The Chemistry of Bioluminescence: An Analysis of Chemical Functionalities

Identifieur interne : 000564 ( Main/Exploration ); précédent : 000563; suivant : 000565

The Chemistry of Bioluminescence: An Analysis of Chemical Functionalities

Auteurs : Isabelle Navizet [Afrique du Sud] ; Ya-Jun Liu [République populaire de Chine] ; Nicolas Ferré [France] ; Daniel Roca-Sanjuán [Suède] ; Roland Lindh [Suède]

Source :

RBID : ISTEX:A33CAD88FB5F480C9F1FCFD293CABF39EF2EB208

English descriptors

Abstract

Firefly luciferase is one of the most studied bioluminescent systems, both theoretically and experimentally. Herein we review the current understanding of the bioluminescent process from a chemical functionality perspective based on those investigations. Three key components are emphasized: the chemiluminophore, the electron‐donating fragment, and how these are affected by the substrate–enzyme interaction. The understanding is based on details of how the peroxide OO bond supports the production of electronically excited products and how the charge‐transfer (CT) mechanism, with the aid of an electron‐donating group, lowers the activation barrier to support a reaction occurs in living organisms. For the substrate–enzyme complex it is demonstrated that the enzyme can affect the hydrogen‐bonding around the CT‐controlling group, resulting in a mechanism for color modulation. Finally, we analyse other luciferin–luciferase systems and compare them to the key chemical functionalities of the fragments of the luciferin–luciferase complex with respect to similarities and differences.
Evolution of oxyluciferin: Starting from simple models expanding to more complex ones (see picture) this review shows how theoretical calculations give insights for the color modulation of firefly luciferin.

Url:
DOI: 10.1002/cphc.201100504


Affiliations:


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<front>
<div type="abstract" xml:lang="en">Firefly luciferase is one of the most studied bioluminescent systems, both theoretically and experimentally. Herein we review the current understanding of the bioluminescent process from a chemical functionality perspective based on those investigations. Three key components are emphasized: the chemiluminophore, the electron‐donating fragment, and how these are affected by the substrate–enzyme interaction. The understanding is based on details of how the peroxide OO bond supports the production of electronically excited products and how the charge‐transfer (CT) mechanism, with the aid of an electron‐donating group, lowers the activation barrier to support a reaction occurs in living organisms. For the substrate–enzyme complex it is demonstrated that the enzyme can affect the hydrogen‐bonding around the CT‐controlling group, resulting in a mechanism for color modulation. Finally, we analyse other luciferin–luciferase systems and compare them to the key chemical functionalities of the fragments of the luciferin–luciferase complex with respect to similarities and differences.</div>
<div type="abstract" xml:lang="en">Evolution of oxyluciferin: Starting from simple models expanding to more complex ones (see picture) this review shows how theoretical calculations give insights for the color modulation of firefly luciferin.</div>
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