Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca<sup>2+</sup>‐regulated Photoproteins of Different Organisms

Eremeeva, Elena V.; Барцев, С. И.; Berkel, Willem J.H. van; Vysotski, Eugene S.

doi:10.1111/php.12664

Cited by 10 publications

(7 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The obelin bioluminescence is thus red-shifted with respect to aequorin. Furthermore, their light emission kinetics and sensitivity to calcium concentration differ. , Another interesting observation is that when excited, aequorin is able to transfer its stored energy to a green fluorescent protein (GFP), which eventually emits a green light; in the absence of GFP, aequorin emits a blue light . These facts demonstrate once again the role of the protein environment in the color modulation of the emitted light.…”

Section: Ante Et Post Chemiexcitationmentioning

confidence: 99%

Chemi- and Bioluminescence of Cyclic Peroxides

et al. 2018

View full text Add to dashboard Cite

Bioluminescence is a phenomenon that has fascinated mankind for centuries. Today the phenomenon and its sibling, chemiluminescence, have impacted society with a number of useful applications in fields like analytical chemistry and medicine, just to mention two. In this review, a molecular-orbital perspective is adopted to explain the chemistry behind chemiexcitation in both chemi- and bioluminescence. First, the uncatalyzed thermal dissociation of 1,2-dioxetane is presented and analyzed to explain, for example, the preference for triplet excited product states and increased yield with larger nonreactive substituents. The catalyzed fragmentation reaction and related details are then exemplified with substituted 1,2-dioxetanone species. In particular, the preference for singlet excited product states in that case is explained. The review also examines the diversity of specific solutions both in Nature and in artificial systems and the difficulties in identifying the emitting species and unraveling the color modulation process. The related subject of excited-state chemistry without light absorption is finally discussed. The content of this review should be an inspiration to human design of new molecular systems expressing unique light-emitting properties. An appendix describing the state-of-the-art experimental and theoretical methods used to study the phenomena serves as a complement.

show abstract

Section: Ante Et Post Chemiexcitationmentioning

confidence: 99%

Chemi- and Bioluminescence of Cyclic Peroxides

et al. 2018

View full text Add to dashboard Cite

show abstract

“…If this is the case then Ca 2+ ‐binding sites with the highest affinity to Ca 2+ can have different location in different Ca 2+ ‐regulated photoproteins. Since Ca 2+ ‐binding sites of highest affinity bind calcium ion in the first instance, it brings about dissimilar order of calcium binding in the different photoproteins and consequently could mainly account for the revealed distinctions in light emission kinetics and sensitivity to calcium of photoproteins originated from different organisms 14,41 …”

Section: Resultsmentioning

confidence: 99%

“…Since Ca 2+binding sites of highest affinity bind calcium ion in the first instance, it brings about dissimilar order of calcium binding in the different photoproteins and consequently could mainly account for the revealed distinctions in light emission kinetics and sensitivity to calcium of photoproteins originated from different organisms. 14,41 Of note is that in all Ca 2+ -regulated photoproteins the C-terminus caps the substrate-binding cavity, ensuring a solvent-inaccessible and nonpolar environment of the CTZ derivative. 29,42,43 The inaccessibility of the internal substrate-binding cavity of photoproteins to solvent is additionally secured by the hydrogen bond interactions between helix A residues and residues from helix H and the C-terminus.…”

Section: Overall Structure Of Obelin-vmentioning

confidence: 99%

Crystal structure of semisynthetic obelin‐v

Larionova

Eremeeva

et al. 2021

Protein Science

Self Cite

View full text Add to dashboard Cite

Coelenterazine-v (CTZ-v), a synthetic derivative with an additional benzyl ring, yields a bright bioluminescence of Renilla luciferase and its "yellow" mutant with a significant shift in the emission spectrum toward longer wavelengths, which makes it the substrate of choice for deep tissue imaging. Although Ca 2+ -regulated photoproteins activated with CTZ-v also display red-shifted light emission, in contrast to Renilla luciferase their bioluminescence activities are very low, which makes photoproteins activated by CTZ-v unusable for calcium imaging. Here, we report the crystal structure of Ca 2+ -regulated photoprotein obelin with 2-hydroperoxycoelenterazine-v (obelin-v) at 1.80 Å resolution. The structures of obelin-v and obelin bound with native CTZ revealed almost no difference; only the minor rearrangement in hydrogen-bond pattern and slightly increased distances between key active site residues and some atoms of 2-hydroperoxycoelenterazine-v were found. The fluorescence quantum yield (Φ FL ) of obelin bound with coelenteramide-v (0.24) turned out to be even higher than that of obelin with native coelenteramide (0.19). Since both obelins are in effect the enzyme-substrate complexes containing the 2-hydroperoxy adduct of CTZ-v or CTZ, we reasonably assume the chemical reaction mechanisms and the yields of the reaction products (Φ R ) to be similar for both obelins. Based on these findings we suggest that low bioluminescence activity of obelin-v is caused by the low efficiency of generating an electronic excited state (Φ S ). In turn, the low Φ S value as compared to that of native CTZ might be the result of small changes in the substrate microenvironment in the obelin-v active site.

show abstract

“…In addition, the decay kinetics of this aequorin variant was satisfactorily described by a two-exponential decay function and consequently by two rate constants—“fast” ( k 1 ) and “slow” ( k 2 ), i.e., similar to all studied obelins ( Table 5 ). According to the recently proposed unanimous kinetic model for photoprotein bioluminescence, which incorporates the “positive cooperativity” between the Ca 2+ -binding sites II and III [ 44 ], the fast decay component of bioluminescence was attributed to the intermediate that arises after calcium binding with the unpaired N-terminal Ca 2+ -binding site I. Thus, appearance of the “fast” component in the decay kinetics of light signal of Aq_A6 might be attributed to significant structural changes in the N-terminal domain, owing to the coelenterazine analogue used as a substrate.…”

Section: Resultsmentioning

confidence: 99%

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents

Eremeeva

Jiang

Malikova

et al. 2020

IJMS

Self Cite

View full text Add to dashboard Cite

Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial. In this paper, we investigated the specific bioluminescence activity, light emission spectra, stopped-flow kinetics and sensitivity to calcium of the semi-synthetic aequorins and obelins activated by novel coelenterazine analogues and the recently reported coelenterazine derivatives. Several semi-synthetic photoproteins activated by the studied coelenterazine analogues displayed sufficient bioluminescence activities accompanied by various changes in the spectral and kinetic properties as well as in calcium sensitivity. The poor activity of certain semi-synthetic photoproteins might be attributed to instability of some coelenterazine analogues in solution and low efficiency of 2-hydroperoxy adduct formation. In most cases, semi-synthetic obelins and aequorins displayed different properties upon being activated by the same coelenterazine analogue. The results indicated that the OH-group at the C-6 phenyl ring of coelenterazine is important for the photoprotein bioluminescence and that the hydrogen-bond network around the substituent in position 6 of the imidazopyrazinone core could be the reason of different bioluminescence activities of aequorin and obelin with certain coelenterazine analogues.

show abstract

Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca²⁺‐regulated Photoproteins of Different Organisms

Cited by 10 publications

References 57 publications

Chemi- and Bioluminescence of Cyclic Peroxides

Chemi- and Bioluminescence of Cyclic Peroxides

Crystal structure of semisynthetic obelin‐v

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents

Contact Info

Product

Resources

About

Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca2+‐regulated Photoproteins of Different Organisms

Cited by 10 publications

References 57 publications

Chemi- and Bioluminescence of Cyclic Peroxides

Chemi- and Bioluminescence of Cyclic Peroxides

Crystal structure of semisynthetic obelin‐v

Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents

Contact Info

Product

Resources

About

Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca²⁺‐regulated Photoproteins of Different Organisms