Important Site of Luciferin on Firefly Bioluminescence
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Luciferin
Photoprotein
Luciferases
Bioluminescence imaging
Abstract— The chemical steps and the products of the bioluminescent and chemiluminescent oxidations of firefly luciferin are elucidated. The colors of firefly bioluminescence can be explained in terms of different ionic excited states and spectral shifts due to changes in molecular environment. Firefly luciferase undergoes conformational changes during catalysis. There are two sites for light production per 100,000 mW. A regulatory mechanism involving dehydro‐luciferin is proposed for control of firefly flashing.
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The firefly luciferase–luciferin pair is a bright star used for probing in a diverse range of fields.
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Photoprotein
Bioluminescence imaging
Luciferases
Light emission
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Firefly shows bioluminescence by "luciferin−luciferase" (L−L) reaction using luciferin, luciferase, ATP and O2. The chemical photon generation by an enzymatic reaction is widely utilized for analytical methods including biological imaging in the life science fields. To expand photondetecting analyses with firefly bioluminescence, it is important for users to understand the chemical basis of the L−L reaction. In particular, the emission color variation of the L−L reaction is one of the distinguishing characteristics for multicolor luciferase assay and in vivo imaging. From the viewpoint of fundamental chemistry, this review explains the recent progress in the studies on the molecular mechanism of emission color variation after showing the outline of the reaction mechanism of the whole L−L reaction. On the basis of the mechanism, the progresses in organic synthesis of luciferin analogs modulating their emission colors are also presented to support further developments of red/near infrared in vivo biological imaging utility of firefly bioluminescence. Keywords: Firefly, Bioluminescence, Luciferase, Luciferin, Multicolor assay, NIR spectroscopy, In vivo imaging.
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Firefly bioluminescence, which produces high-efficiency light, is widely used in life science applications. For in vivo bioluminescence imaging, the near-infrared range (650–900 nm) is suitable because of its high permeability in deep biological tissues. In this study, we synthesized new luciferin analogues that emit light at 765 nm using Photinus pyralis luciferase. Firefly bioluminescence, which produces high-efficiency light, is widely used in life science applications. For in vivo bioluminescence imaging, the near-infrared range (650–900 nm) is suitable because of its high permeability in deep biological tissues. In this study, we synthesized new luciferin analogues that emit light at 765 nm using Photinus pyralis luciferase.
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Firefly bioluminescence is widely used in life science research as a useful analysis tool. For example, the adenosine-5′-triphosphate (ATP)-dependent enzymatic firefly bioluminescence reaction has long been utilized as a microbial monitoring tool. Rapid and sensitive firefly luciferin-luciferase combinations are used not only to measure cell viability but also for reporter-gene assays. Recently, bioluminescence was utilized as a noninvasive, real-time imaging tool for living subjects to monitor cells and biological events. However, the number of commercialized luciferase genes is limited and tissue-permeable near-infrared (NIR) region emitting light is required for in vivo imaging. In this review, recent studies describing synthetic luciferin analogues predicted to have red-shifted bioluminescence are summarized. Luciferase substrates emitting red, green, and blue light that were designed and developed in our laboratory are presented. The longest emission wavelength of the synthesized luciferin analogues was recorded at 675 nm, which is within the NIR region. This compound is now commercially available as "Aka Lumine®". Keywords: Biological window, Bioluminescence imaging, Enhanced emission, Firefly, Luciferin analogue, Multicolor emission, Near-infrared.
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Abstract There is growing interest in applying bioluminescence for imaging varies biological processes in life sciences due to its high resolution, selectivity, and signal/noise ratio (no need of external light excitation). Among the diverse bioluminescence systems, firefly luciferin–luciferase system is considered to be the most popular one for bioimaging applications both in vitro and in vivo. The general design strategy of this system is to cage luciferin (i. e., free luciferin is protected with distinctive functional groups). When the protecting moieties are removed by their corresponding analytes, bioluminescence signal turns “on”, enabling people to understand their biological processes. Considering that d ‐luciferin‐luciferase bioluminescence imaging system is now becoming a hot and cutting‐edge research topic, in this minireview, we briefly explain the bioluminescence mechanism and summarize the biological molecule‐responsive, d ‐luciferin‐based bioluminescence imaging probes. Moreover, the attempts to optimize the photochemical properties of d ‐luciferin are also introduced. Current challenges and future perspectives for activity‐based luciferase‐luciferin bioluminescence system are also outlooked. With the understanding of the structure−property relationships and working mechanisms of these bioluminescence probes, we hope that this minireview might provide effective guidance for the development of bioluminescence imaging probes and even their clinical translations.
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Luciferases
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Bioluminescence imaging
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Abstract The New Zealand glowworm, Arachnocampa luminosa , is well-known for displays of blue-green bioluminescence, but details of its bioluminescent chemistry have been elusive. The glowworm is evolutionarily distant from other bioluminescent creatures studied in detail, including the firefly. We have isolated and characterised the molecular components of the glowworm luciferase-luciferin system using chromatography, mass spectrometry and 1 H NMR spectroscopy. The purified luciferase enzyme is in the same protein family as firefly luciferase (31% sequence identity). However, the luciferin substrate of this enzyme is produced from xanthurenic acid and tyrosine, and is entirely different to that of the firefly and known luciferins of other glowing creatures. A candidate luciferin structure is proposed, which needs to be confirmed by chemical synthesis and bioluminescence assays. These findings show that luciferases can evolve independently from the same family of enzymes to produce light using structurally different luciferins.
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Lampyridae
Photoprotein
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Bioluminescence and chemiluminescence studies were used to measure the amount of adenosine triphosphate and therefore the amount of energy available. Firefly luciferase - luciferin enzyme system was emphasized. Photometer designs are also considered.
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Photometer
Luciferases
Photoprotein
Luminescent Measurements
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