Recombinant light-sensitive photoprotein berovin from ctenophore Beroe abyssicola: Bioluminescence and absorbance characteristics.

Autor: Burakova LP; Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, Russia; Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russia., Kolmakova AA; Analytical Laboratory, Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, Russia., Vysotski ES; Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Krasnoyarsk, Russia. Electronic address: eugene_vysotski@ibp.ru.
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Oct 08; Vol. 624, pp. 23-27. Date of Electronic Publication: 2022 Jul 22.
DOI: 10.1016/j.bbrc.2022.07.079
Abstrakt: The bright bioluminescence of ctenophores inhabiting the oceans worldwide is caused by light-sensitive Ca 2+ -regulated photoproteins. By now, the cDNAs encoding photoproteins from the four different ctenophore species have been cloned and the recombinant proteins have been characterized to some extent. In this work, we report on the specific activity and the quantum yield of bioluminescence reaction as well as the absorbance characteristics of high-purity recombinant berovin. To determine those, we applied the amino acid composition analysis to accurately measure berovin concentration and the recombinant aequorin as a light standard to convert relative light units to quanta. The extinction coefficient of 1% berovin solution at 435 nm was found to be 1.82. The one can be employed to precisely determine the protein concentration of active photoproteins from other ctenophore species. The specific activity and the bioluminescence quantum yield were respectively found to be 1.98 × 10 15 quanta/mg and 0.083. These values appeared to be several times lower than those of the cnidarian photoproteins, which is obviously due to differences in amino acid environments of the substrate in active sites of these photoproteins.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2022 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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