» Articles » PMID: 15345564

Incoherent Manipulation of the Photoactive Yellow Protein Photocycle with Dispersed Pump-dump-probe Spectroscopy

Overview
Journal Biophys J
Publisher Cell Press
Specialty Biophysics
Date 2004 Sep 4
PMID 15345564
Citations 29
Authors
Affiliations
Soon will be listed here.
Abstract

Photoactive yellow protein is the protein responsible for initiating the "blue-light vision" of Halorhodospira halophila. The dynamical processes responsible for triggering the photoactive yellow protein photocycle have been disentangled with the use of a novel application of dispersed ultrafast pump-dump-probe spectroscopy, where the photocycle can be started and interrupted with appropriately tuned and timed laser pulses. This "incoherent" manipulation of the photocycle allows for the detailed spectroscopic investigation of the underlying photocycle dynamics and the construction of a fully self-consistent dynamical model. This model requires three kinetically distinct excited-state intermediates, two (ground-state) photocycle intermediates, I(0) and pR, and a ground-state intermediate through which the protein, after unsuccessful attempts at initiating the photocycle, returns to the equilibrium ground state. Also observed is a previously unknown two-photon ionization channel that generates a radical and an ejected electron into the protein environment. This second excitation pathway evolves simultaneously with the pathway containing the one-photon photocycle intermediates.

Citing Articles

Watching a signaling protein function: What has been learned over four decades of time-resolved studies of photoactive yellow protein.

Schotte F, Cho H, Dyda F, Anfinrud P Struct Dyn. 2024; 11(2):021303.

PMID: 38595979 PMC: 11003764. DOI: 10.1063/4.0000241.


Biological function investigated by time-resolved structure determination.

Schmidt M Struct Dyn. 2023; 10(1):010901.

PMID: 36846099 PMC: 9946696. DOI: 10.1063/4.0000177.


Reaction Dynamics in the Chrimson Channelrhodopsin: Observation of Product-State Evolution and Slow Diffusive Protein Motions.

van Stokkum I, Hontani Y, Vierock J, Krause B, Hegemann P, Kennis J J Phys Chem Lett. 2023; 14(6):1485-1493.

PMID: 36745035 PMC: 9940203. DOI: 10.1021/acs.jpclett.2c03110.


Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein.

Konold P, Arik E, Weissenborn J, Arents J, Hellingwerf K, van Stokkum I Nat Commun. 2020; 11(1):4248.

PMID: 32843623 PMC: 7447820. DOI: 10.1038/s41467-020-18065-9.


Towards symmetry driven and nature inspired UV filter design.

Horbury M, Holt E, Mouterde L, Balaguer P, Cebrian J, Blasco L Nat Commun. 2019; 10(1):4748.

PMID: 31628301 PMC: 6802189. DOI: 10.1038/s41467-019-12719-z.


References
1.
Kort R, Hoff W, Van West M, Kroon A, Hoffer S, Vlieg K . The xanthopsins: a new family of eubacterial blue-light photoreceptors. EMBO J. 1996; 15(13):3209-18. PMC: 451869. View

2.
Ujj L, Devanathan S, Meyer T, Cusanovich M, Tollin G, Atkinson G . New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy. Biophys J. 1998; 75(1):406-12. PMC: 1299710. DOI: 10.1016/S0006-3495(98)77525-3. View

3.
Unno M, Kumauchi M, Sasaki J, Tokunaga F, Yamauchi S . Resonance Raman spectroscopy and quantum chemical calculations reveal structural changes in the active site of photoactive yellow protein. Biochemistry. 2002; 41(17):5668-74. DOI: 10.1021/bi025508o. View

4.
Xie A, Hoff W, Kroon A, Hellingwerf K . Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein. Biochemistry. 1996; 35(47):14671-8. DOI: 10.1021/bi9623035. View

5.
Imamoto Y, Kataoka M, Tokunaga F, Asahi T, Masuhara H . Primary photoreaction of photoactive yellow protein studied by subpicosecond-nanosecond spectroscopy. Biochemistry. 2001; 40(20):6047-52. DOI: 10.1021/bi002437p. View