Perspectives on Bioluminescence Mechanisms

Lee, John

doi:10.1111/php.12650

Cited by 32 publications

(32 citation statements)

References 150 publications

(249 reference statements)

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“…[15], to identify, analyse, and calculate the residues with error values, while PROCHECK http://services.mbi.ucla.edu/PROCHECK/ [16], and Verify3D http://services.mbi.ucla.edu/Verify_3D/ [17] were used to check the accuracy and validation of the modelled 3D structures.…”

Section: Homology Model Validationmentioning

confidence: 99%

Structural Characterization of Novel Luciferase from Bioluminescence Fungi Verticillium longisporum

Yarima

Sambo

Kwairanga

et al. 2020

BJI

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Luciferase is an enzyme that catalyses a reaction to produce a visible light using an oxidative process, a chemical reaction that is typically referred to as bioluminescent. Insects, bacterial origin or microorganism of marine nature were considered as the mainly sources of discovered luciferase. The protein was commercialized for biomedical and biotechnological use as reporter gene. The first discovered wild form of luciferase originally from Photinu spyralis (firefly). Hence, there is need for both exploration and examination of novel luciferase to be expanded to new sources such as fungal which may likely be exploited to serve commercial purposes and applications. In this study, a novel uncharacterized luciferase protein from a fungal species Verticillium longisporum, was modelled and analysed using bioinformatic tools. The modelled 3D structure is of high quality with a PROCHECK score of 99.5%, ERRAT2 value of 91.01%, and Verify3D score of91.01%, showing that the conformational structure is acceptable. The result showed that the fungal luciferase enzyme share major characteristics with luciferase representative from various fungal and bacterial species. There is only a slight difference in the two nucleotide bindings in V. longisporum with a D/E substitution of D with E and S/T substitution. The difference of the two nucleotides binding from the two proteins may be related to the evolutionary trends. Other differences include increased number of hydrophobic and polar amino acid groups than aromatic and aliphatic ones, as well as more coils and loops with less strands. The distance between the ligand and the binding site that houses Asp 64 and Thr 110 from template proteins (Riboflavin lyaseRcaE) and Asp 543 and Thr 589 from model luciferase is similar. The only difference occurred in the V. longisporum; protein oxidoreductase activities acts on paired donors, incorporate or reduce molecular oxygen, while in the template protein oxidoreductase activities act on single donors with incorporation of molecular oxygen. This study on fungal sourced luciferase present a unique opportunity away from the more well established bacterial and insect based luciferase.

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Section: Homology Model Validationmentioning

confidence: 99%

Structural Characterization of Novel Luciferase from Bioluminescence Fungi Verticillium longisporum

Yarima

Sambo

Kwairanga

et al. 2020

BJI

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“…The reactions are Ca-dependent, and this is a basis for their biomedical application [34][35]. Biochemical and photophysical mechanisms of the bioluminescence reactions [36][37][38][39][40][41] and spectral characteristics of their products -coelenteramide-containing proteins [42][43][44][45][46][47][48][49] are under intensive investigations now.…”

Section: Introductionmentioning

confidence: 99%

Low-intensity Exposures via Luminescent Bioassays of Different Complexity: Cells, Enzyme Reactions and Fluorescent Proteins

Kudryasheva¹,

Kovel²

2019

Preprint

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Current paper reviews applications of luminescence bioassays for monitoring low-intensity factors, namely, radioactivity of different types (alpha, beta and gamma), and bioactive compounds (humic substances and fullerenols). Luminescence intensity is taken as a physiological parameter of luminous organisms. High rates of luminescence response can provide (1) a proper number of experiments under comparable conditions and, therefore, proper statistical processing, with this being highly important for ‘noisy’ low-dose exposures; (2) non-genetic, i.e. biochemical and physicochemical mechanisms of cellular response, in accordance to “exposome” concept. Bioassays based on luminous marine bacteria, their enzymes, and fluorescence coelenteramide-containing proteins were used to compare results of low-intensity exposures at cellular, biochemical and physicochemical levels, respectively. Results of the cellular exposures were discussed in terms of hormesis concept. Bioluminescence time dependence under low-dose radiation exposures corresponded to hormesis or threshold models; no bioluminescence monotonic dependency on intensity of exposure (dose rate, radioactivity, concentration) was found. Bioluminescence activation and absence of its dependency on intensity of exposure can be accepted as features of cellular adaptive response. Changes of biological luminescence were analyzed and discussed for bioassays of lower organization level – enzymes and florescent protein.

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“…Clearly, these quantum yields must all be <1.0. The firefly system is the one reported with highest bioluminescence, Φ B = 0.61, with Φ F ~ 0.7 . The chemiluminescence models for bacterial bioluminescence reported in the literature have very low Φ C and deserve cautious interpretation due to the probability of competing side reactions for these oxidation reactions of high exothermicity.…”

Section: Introductionmentioning

confidence: 99%

“…The intermediacy of the HEI as a dioxetanone in the bioluminescence of firefly and cypridinid luciferins was quickly extended to other bioluminescences that employ imidopyrazinone luciferins, commonly coelenterazine . There followed also much enthusiasm for the synthesis of cyclic peroxide compounds having bright chemiluminescence and many discovered have a Φ C comparable to the high Φ B of firefly.…”

Section: Introductionmentioning

confidence: 99%

The Sensitized Bioluminescence Mechanism of Bacterial Luciferase

Lee

Müller²,

Visser

2018

Photochem & Photobiology

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After more than one‐half century of investigations, the mechanism of bioluminescence from the FMNH2 assisted oxygen oxidation of an aliphatic aldehyde on bacterial luciferase continues to resist elucidation. There are many types of luciferase from species of bioluminescent bacteria originating from both marine and terrestrial habitats. The luciferases all have close sequence homology, and in vitro, a highly efficient light generation is obtained from these natural metabolites as substrates. Sufficient exothermicity equivalent to the energy of a blue photon is available in the chemical oxidation of the aldehyde to the corresponding carboxylic acid, and a luciferase‐bound FMNH‐OOH is a key player. A high energy species, the source of the exothermicity, is unknown except that it is not a luciferin cyclic peroxide, a dioxetanone, as identified in the pathway of the firefly and the marine bioluminescence systems. Besides these natural substrates, variable bioluminescence properties are found using other reactants such as flavin analogs or aldehydes, but results also depend on the luciferase type. Some rationalization of the mechanism has resulted from spatial structure determination, NMR of intermediates and dynamic optical spectroscopy. The overall light path appears to fall into the sensitized class of chemiluminescence mechanism, distinct from the dioxetanone types.

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Perspectives on Bioluminescence Mechanisms

Cited by 32 publications

References 150 publications

Structural Characterization of Novel Luciferase from Bioluminescence Fungi Verticillium longisporum

Structural Characterization of Novel Luciferase from Bioluminescence Fungi Verticillium longisporum

Low-intensity Exposures via Luminescent Bioassays of Different Complexity: Cells, Enzyme Reactions and Fluorescent Proteins

The Sensitized Bioluminescence Mechanism of Bacterial Luciferase

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