Femtosecond and picosecond dynamics of recombinant bacteriorhodopsin primary reactions compared to the native protein in trimeric and monomeric forms

O. A. Smitienko; O. V. Nekrasova; A. V. Kudriavtsev; M. A. Yakovleva; I. V. Shelaev; F. E. Gostev; D. A. Dolgikh; I. B. Kolchugina; V. A. Nadtochenko; M. P. Kirpichnikov; T. B. Feldman; M. A. Ostrovsky

doi:10.1134/S0006297917040113

Femtosecond and picosecond dynamics of recombinant bacteriorhodopsin primary reactions compared to the native protein in trimeric and monomeric forms

Авторлар: Smitienko O.¹, Nekrasova O.²^,3, Kudriavtsev A.¹^,3, Yakovleva M.¹, Shelaev I.⁴, Gostev F.⁴, Dolgikh D.²^,3^,5, Kolchugina I.³, Nadtochenko V.⁴, Kirpichnikov M.²^,3, Feldman T.¹^,3^,5, Ostrovsky M.¹^,3
Мекемелер:
1. Emanuel Institute of Biochemical Physics
2. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
3. Lomonosov Moscow State University
4. Semenov Institute of Chemical Physics
5. Pirogov Russian National Research Medical University
Шығарылым: Том 82, № 4 (2017)
Беттер: 490-500
Бөлім: Article
URL: https://journals.rcsi.science/0006-2979/article/view/151351
DOI: https://doi.org/10.1134/S0006297917040113
ID: 151351

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Photochemical reaction dynamics of the primary events in recombinant bacteriorhodopsin (bR_rec) was studied by femtosecond laser absorption spectroscopy with 25-fs time resolution. bR_rec was produced in an Escherichia coli expression system. Since bR_rec was prepared in a DMPC–CHAPS micelle system in the monomeric form, its comparison with trimeric and monomeric forms of the native bacteriorhodopsin (bR_trim and bR_mon, respectively) was carried out. We found that bR_rec intermediate I (excited state of bR) was formed in the range of 100 fs, as in the case of bR_trim and bR_mon. Further processes, namely the decay of the excited state I and the formation of intermediates J and K of bR_rec, occurred more slowly compared to bR_trim, but similarly to bR_mon. The lifetime of intermediate I, judging from the signal of ΔA_ESA(470-480 nm), was 0.68 ps (78%) and 4.4 ps (22%) for bR_rec, 0.52 ps (73%) and 1.7 ps (27%) for bR_mon, and 0.45 ps (90%) and 1.75 ps (10%) for bR_trim. The formation time of intermediate K, judging from the signal of ΔA_GSA(625-635 nm), was 13.5 ps for bR_rec, 9.8 ps for bR_mon, and 4.3 ps for bR_trim. In addition, there was a decrease in the photoreaction efficiency of bR_rec and bR_mon as seen by a decrease in absorbance in the differential spectrum of the intermediate K by ~14%. Since photochemical properties of bR_rec are similar to those of the monomeric form of the native protein, bR_rec and its mutants can be considered as a basis for further studies of the mechanism of bacteriorhodopsin functioning.

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bacteriorhodopsin, recombinant protein, primary reactions, femtosecond absorption laser spectroscopy

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Femtosecond and picosecond dynamics of recombinant bacteriorhodopsin primary reactions compared to the native protein in trimeric and monomeric forms

Толық мәтін

Аннотация

Негізгі сөздер

Авторлар туралы

O. Smitienko

O. Nekrasova

A. Kudriavtsev

M. Yakovleva

I. Shelaev

F. Gostev

D. Dolgikh

I. Kolchugina

V. Nadtochenko

M. Kirpichnikov

T. Feldman

M. Ostrovsky

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