Header Image Title: THE ROLE OF BACTERIORHODOPSIN IN LIGHT HARVESTING AND ATP PRODUCTION BY HALOBACTERIUM SALINARUM CELLS
Peer-reviewed articles 17,970 +
ARTICLE METRICS


Altmetrics info

Title: THE ROLE OF BACTERIORHODOPSIN IN LIGHT HARVESTING AND ATP PRODUCTION BY HALOBACTERIUM SALINARUM CELLS
THE ROLE OF BACTERIORHODOPSIN IN LIGHT HARVESTING AND ATP PRODUCTION BY HALOBACTERIUM SALINARUM CELLS
Gabi Drochioiu
10.5593/sgem2022/6.1/s25.17
10.5593/sgem2022/6.1
1314-2704
978-619-7603-48-4
English
22
6.1
•    Prof. DSc. Oleksandr Trofymchuk, UKRAINE 
•    Prof. Dr. hab. oec. Baiba Rivza, LATVIA
Advances in Biotechnology
Halobacterium salinarum is an extremely halophilic marine Gram-negative obligate aerobic archaeon. Despite its name, this is not a bacterium, but rather a member of the domain Archaea, which lives in hypersaline lakes. Bacteriorhodopsin (BRh) is the red retinal-containing protein found in the cell membranes of H. salinarum and is considered a light-activated proton pump that transports protons across the plasma membrane. Bacteriorhodopsin photointermediates have been defined in kinetic and spectroscopic terms as BR568, K590, L550, M412, N560, and O640. We have previously shown, using the Forster cycle for BRh that its acidity increases greatly on illumination. Therefore, protons released upon illumination of the L550 intermediate with 412 nm light may not play an essential role in ATP production. Instead, the light-induced excitation energy, which represents the energy difference between the L550 and M412 states, can be used to extract an ATP molecule attached to ATP synthase. Thus, we have shown that this amount of energy corresponds to a near-infrared vibration, which is sufficient for ATP production and provides the most feasible molecular mechanism for this phenomenon. Here, we provide new evidence that protons are released due to BRh excitation, unrelated to ATP synthesis, being only a secondary phenomenon. In addition, once released from H. salinarum cells, protons should return back into the cells via ATP-synthase molecules to produce ATP. This is not possible at pH > 7.0, such as pH 9.5. However, the stability of M intermediates and ATP formation appear to be increased at higher pH values. Indeed, a spectral shift of 138 nm may be associated with an energy amount of about 17 kcal mol-1, which is enough energy to release a mole of ATP from ATP-synthase. In general, light excitation of fluorescent molecules is a phenomenon that induces a strong increase in their acidity. Recent data suggest that the chemiosmotic hypothesis put forward by Peter Mitchell to explain ATP formation in living cells is not correct, at least in terms of explaining light-induced ATP production in H. salinarum cells.
Bacteriorhodopsin, Halobacterium salinarum, ATP production, Forster cycle, Proton release
[1] DasSarma S., Extreme microbes: salt-loving microorganisms are helping biologists understand the unifying features of life and molecular secrets of survival under extreme conditions. American Scientist, vol. 95/issue 3, pp. 224-232, 2007;
[2] Singh P., Singh S., Jaggi N., Kim K.H., Devi, P., Recent advances in bacteriorhodopsin-based energy harvesters and sensing devices. Nano Energy, vol. 79, 105482, 2021.
[3] Hirai T., Subramaniam S., Structural insights into the mechanism of proton pumping by Bacteriorhodopsin. FEBS Letters, vol. 545/issue 1, pp. 2-8, 2003;
[4] Subramaniam S., Lindahl M., Bullough P., Faruqi A.R., Tittor J., Oesterhelt D., Brown L., Lanyi J., Henderson, R., Protein conformational changes in the bacteriorhodopsin photocycle. Journal of molecular biology, vol. 287/issue 1, pp. 145- 161, 1999.
[5] Drochioiu G., Closca C.M., Ion L., Pelin I., Gradinaru R.V., Bacteriorhodopsin from Halobacterium salinarum is a key compound of Bioenergetics. International Multidisciplinary Scientific GeoConference: SGEM2019, Bulgaria, vol. 19/issue 6.1, pp. 575-582, 2019.
[6] Kaupp G., Photochemische Umlagerungen und Fragmentierungen von Benzol-Derivaten und anellierten Arenen. Angewandte Chemie, vol. 92/issue 4, pp. 245-276, 2008;
[7] Rammelsberg R., Huhn G., Gerwert K., Bacteriorhodopsin's intramolecular protonrelease pathway consists of a hydrogen-bonded network. Biochemistry, vol. 37/issue 14, pp. 5001-5009, 1998.
[8] Friedrich D., Brunig F.N., Nieuwkoop A.J., Netz R.R., Hegemann P., Oschkinat H., Collective exchange processes reveal an active site proton cage in bacteriorhodopsin. Communications Biology, vol. 3/issue 1, pp. 1-9, 2020.
[9] Roy S., Sethi P., Topolancik J., Vollmer, F., All-optical reversible logic gates with optically controlled bacteriorhodopsin protein-coated microresonators. Advances in Optical Technologies, Art. ID 727206, 12 pp., 2012;
[10] Wang L., Shen Z., Wang J., Li B., Chen F., Yang W., Feng X. The pH-dependence of photochemical intermediates of O and P in bacteriorhodopsin by continuous light. Biochemical and biophysical research communications, vol. 343/issue 3, pp. 899- 903, 2006;
[11] Boyer P.D., Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group protonation?. Trends in Biochemical Sciences, vol. 13/issue 1, pp 5-7, 1988;
[12] Kouyama T., Ihara K. Existence of two substates in the O intermediate of the bacteriorhodopsin photocycle. BBA-Biomembranes, vol. 1864/Issue 10, 183998, 2022.
[13] Subramaniam S., Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature, vol. 406/issue 6796, pp. 653-657, 2000.
[14] Shigeta A., Otani Y., Miyasa R., Makino Y., Kawamura I., Okitsu T., Wada A., Naito, A. Photoreaction pathways of bacteriorhodopsin and its D96N mutant as revealed by in situ photoirradiation solid-state NMR. Membranes, vol. 12/issue 3, p. 279, 2022.
Romanian Ministry of Research, Innovation and Digitization, within Program 1— Development of the national RD system, Subprogram 1.2—Institutional Performance— RDI excellence funding projects, Contract no.11PFE/30.12.2021
conference
https://doi.org/10.5593/sgem2022/6.1/s25.17
Download PDF
Proceedings of 22nd International Multidisciplinary Scientific GeoConference SGEM 2022
22nd International Multidisciplinary Scientific GeoConference SGEM 2022, 04 - 10 July, 2022
Proceedings Paper
STEF92 Technology
International Multidisciplinary Scientific GeoConference SGEM
SWS Scholarly Society; Acad Sci Czech Republ; Latvian Acad Sci; Polish Acad Sci; Serbian Acad Sci and Arts; Natl Acad Sci Ukraine; Natl Acad Sci Armenia; Sci Council Japan; European Acad Sci, Arts and Letters; Acad Fine Arts Zagreb Croatia; Croatian Acad Sci and Arts; Acad Sci Moldova; Montenegrin Acad Sci and Arts; Georgian Acad Sci; Acad Fine Arts and Design Bratislava; Turkish Acad Sci.
137-144
04 - 10 July, 2022
website
8645