Intracellular synthesis of<scp>d</scp>-aminoluciferin for bioluminescence generation

Zheng, Zhen; Li, Gongyu; Wu, Chengfan; Zhang, Miaomiao; Zhao, Yue; Liang, Gaolin

doi:10.1039/c7cc00999b

Cited by 16 publications

(13 citation statements)

References 30 publications

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“…Once the GGR moiety was removed from the bioluminescence probe by uPA, the generated aminoluciferin could emit the bioluminescence signal, thus realizing the uPA imaging. Based on this strategy, a variety of biological molecule‐responsive bioluminescent probes have been designed and successfully applied to evaluate the activity of enzymes or detect the small molecule compounds, including tyrosinase (TYR), [23] glutathione (GSH), [12b,24] CO, [25] etc., which will be discussed in the following section.…”

Section: D‐luciferin‐based Probes For Bioimagingmentioning

confidence: 99%

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Activity‐Based Luciferase‐Luciferin Bioluminescence System for Bioimaging Applications

et al. 2021

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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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Section: D‐luciferin‐based Probes For Bioimagingmentioning

confidence: 99%

“…Typical method for GSH bioluminescence imaging is to cage d ‐luciferin with disulfide‐based moieties. Upon GSH reduction, the bioluminescence signal of these probes turns “on” intelligently [12b,24] …”

Section: D‐luciferin‐based Probes For Bioimagingmentioning

confidence: 99%

Activity‐Based Luciferase‐Luciferin Bioluminescence System for Bioimaging Applications

et al. 2021

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“…cell proliferation and migration, enzyme activities, proteinprotein interaction, and gene expression). [22][23][24][25][26][27] In the firefly luciferase-luciferin BL system, firefly luciferase catalyzes its highspecific substrate (D-luciferin or 6 0 -aminoluciferin) to emit visible light with the assistance of ATP, O 2 and Mg 2+ . [28,29] Excitation light is not needed in this process, to avoid the inherent disturbances from fluorescence (e.g.…”

Section: Introductionmentioning

confidence: 99%

A caged 2‐hydroxyethyl luciferin for bioluminescence imaging of nitroxyl in living cells

Wang

et al. 2020

Luminescence

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Nitroxyl (HNO), a one‐electron reduction product of nitric oxide, demonstrates distinct biological and pharmacological activities. Here we designed a bioluminescent turn‐on probe, HNO‐8, that could be used to visualize HNO without the need for excitation light. HNO‐8 was prepared by caging 2‐hydroxyethyl luciferin with a triphenylphosphine unit, in which 2‐hydroxyethyl luciferin as a novel substrate of firefly luciferase was characterized by stronger and more sustained bioluminescent signals than the most popular substrates of d‐luciferin and 6′‐aminoluciferin. In vitro experiments showed that HNO‐8 could selectively respond to HNO generated from Angeli's salt(AS) in the range 1–50 μM, with a limit of detection of 0.196 μM. The probe was successfully applied for visualizing HNO in luciferase‐transfected Huh7 cancer cells. We envision that HNO‐8 could be used as a powerful bioluminescent sensor for researching HNO biological roles.

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“…In fact, there is no doubt that L‐luciferin changes into D‐luciferin via luciferase and luciferyl‐CoA thioesterase. Thus, a theoretical calculation to prove the occurrence of step 3 is not very necessary since L‐cysteine conversion into D‐luciferin has been verified by HPLC analysis, and recently, a D‐luciferin analogue was intracellularly synthesized from a L‐cysteine complex molecule . Moreover, firefly luciferase can indeed produce light by the catalysis of L‐luciferin in the presence of cofactors .…”

Section: Introductionmentioning

confidence: 99%

“…Thus, a theoretical calculation to prove the occurrence of step 3 is not very necessary since L-cysteine conversion into D-luciferin has been verified by HPLC analysis, [38] and recently, a D-luciferin analogue was intracellularly synthesized from a L-cysteine complex molecule. [39] Moreover, firefly luciferase can indeed produce light by the catalysis of L-luciferin in the presence of cofactors. [40] Therefore, we focus this theoretical study on the details and mechanisms of the first two steps of firefly luciferin regeneration.…”

Section: Introductionmentioning

confidence: 99%

Luciferin Regeneration in Firefly Bioluminescence via Proton‐Transfer‐Facilitated Hydrolysis, Condensation and Chiral Inversion

Cheng

Liu

2019

ChemPhysChem

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Firefly bioluminescence is produced via luciferin enzymatic reactions in luciferase. Luciferin has to be unceasingly replenished to maintain bioluminescence. How is the luciferin reproduced after it has been exhausted? In the early 1970s, Okada proposed the hypothesis that the oxyluciferin produced by the previous bioluminescent reaction could be converted into new luciferin for the next bioluminescent reaction. To some extent, this hypothesis was evidenced by several detected intermediates. However, the detailed process and mechanism of luciferin regeneration remained largely unknown. For the first time, we investigated the entire process of luciferin regeneration in firefly bioluminescence by density functional theory calculations. This theoretical study suggests that luciferin regeneration consists of three sequential steps: the oxyluciferin produced from the last bioluminescent reaction generates 2‐cyano‐6‐hydroxybenzothiazole (CHBT) in the luciferin regenerating enzyme (LRE) via a hydrolysis reaction; CHBT combines with L‐cysteine in vivo to form L‐luciferin via a condensation reaction; and L‐luciferin inverts into D‐luciferin in luciferase and thioesterase. The presently proposed mechanism not only supports the sporadic evidence from previous experiments but also clearly describes the complete process of luciferin regeneration. This work is of great significance for understanding the long‐term flashing of fireflies without an in vitro energy supply.

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Intracellular synthesis ofd-aminoluciferin for bioluminescence generation

Cited by 16 publications

References 30 publications

Activity‐Based Luciferase‐Luciferin Bioluminescence System for Bioimaging Applications

Activity‐Based Luciferase‐Luciferin Bioluminescence System for Bioimaging Applications

A caged 2‐hydroxyethyl luciferin for bioluminescence imaging of nitroxyl in living cells

Luciferin Regeneration in Firefly Bioluminescence via Proton‐Transfer‐Facilitated Hydrolysis, Condensation and Chiral Inversion

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