Molecular Science Institute School of Chemistry, University of the Witwatersrand, PO Wits Johannesburg 2050, South Africa.
Chemphyschem. 2011 Dec 9;12(17):3064-76. doi: 10.1002/cphc.201100504. Epub 2011 Oct 13.
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.
萤火虫荧光素酶是理论和实验研究中最受关注的生物发光系统之一。在此，我们基于这些研究从化学功能的角度综述了对生物发光过程的当前理解。重点强调了三个关键组成部分：化学发光体、供电子片段，以及它们如何受到底物-酶相互作用的影响。这种理解基于过氧化物-O-O-键如何支持产生电子激发产物的细节，以及电荷转移 (CT) 机制如何在供电子基团的帮助下降低激活能垒以支持在生物体中发生反应。对于底物-酶复合物，我们证明了酶可以影响 CT 控制基团周围的氢键，从而产生一种用于调节颜色的机制。最后，我们分析了其他荧光素酶系统，并将它们与荧光素-荧光素酶复合物片段的关键化学功能进行了比较，以了解它们之间的相似和不同之处。
