Early Intermediates in the Photocycle of the Glu46Gln Mutant of Photoactive Yellow Protein: Femtosecond Spectroscopy

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2000 Oct 12

PMID 11023916

Citations 7

Authors

S Devanathan

S Lin

M A Cusanovich

N Woodbury

G Tollin

Affiliations

Soon will be listed here.

Abstract

Transient absorption spectroscopy in the time range from -1 ps to 4 ns, and over the wavelength range from 420 to 550 nm, was applied to the Glu46Gln mutant of the photoactive yellow protein (PYP) from Ectothiorhodospira halophila. This has allowed us to elucidate the kinetic constants of excited state formation and decay and photochemical product formation, and the spectral characteristics of stimulated emission and the early photocycle intermediates. Both the quantum efficiency ( approximately 0.5) and the rate constants for excited state decay and the formation of the initial photochemical intermediate (I(0)) were found to be quite similar to those obtained for wild-type PYP. In contrast, the rate constants for the formation of the subsequent photocycle intermediates (I(0)(double dagger) and I(1)), as well as for I(2) and for ground state regeneration as determined in earlier studies, were found to be from 3- to 30-fold larger. The structural implications of these results are discussed.

Citing Articles

Combined probes of X-ray scattering and optical spectroscopy reveal how global conformational change is temporally and spatially linked to local structural perturbation in photoactive yellow protein.

Kim T, Yang C, Kim Y, Kim J, Kim J, Jung Y Phys Chem Chem Phys. 2016; 18(13):8911-8919.

PMID: 26960811 PMC: 4809902. DOI: 10.1039/c6cp00476h.

Volume-conserving trans-cis isomerization pathways in photoactive yellow protein visualized by picosecond X-ray crystallography.

Jung Y, Lee J, Kim J, Schmidt M, Moffat K, Srajer V Nat Chem. 2013; 5(3):212-20.

PMID: 23422563 PMC: 3579544. DOI: 10.1038/nchem.1565.

On the Configurational and Conformational Changes in Photoactive Yellow Protein that Leads to Signal Generation in Ectothiorhodospira halophila.

Hellingwerf K, Hendriks J, Gensch T J Biol Phys. 2013; 28(3):395-412.

PMID: 23345784 PMC: 3456738. DOI: 10.1023/A:1020360505111.

Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds.

Ihee H, Rajagopal S, Srajer V, Pahl R, Anderson S, Schmidt M Proc Natl Acad Sci U S A. 2005; 102(20):7145-50.

PMID: 15870207 PMC: 1088170. DOI: 10.1073/pnas.0409035102.

Contrasting the excited-state dynamics of the photoactive yellow protein chromophore: protein versus solvent environments.

Vengris M, van der Horst M, Zgrablic G, van Stokkum I, Haacke S, Chergui M Biophys J. 2004; 87(3):1848-57.

PMID: 15345563 PMC: 1304589. DOI: 10.1529/biophysj.104.043224.

References

Meyer T, Tollin G, Hazzard J, Cusanovich M . Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery. Biophys J. 1989; 56(3):559-64. PMC: 1280509. DOI: 10.1016/S0006-3495(89)82703-1. View

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

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

Hoff W, Dux P, Hard K, Devreese B, Crielaard W, Boelens R . Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry. Biochemistry. 1994; 33(47):13959-62. DOI: 10.1021/bi00251a001. View

Hoff W, van Stokkum I, van Ramesdonk H, van Brederode M, Brouwer A, Fitch J . Measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila. Biophys J. 1994; 67(4):1691-705. PMC: 1225531. DOI: 10.1016/S0006-3495(94)80643-5. View

Baca M, Borgstahl G, Boissinot M, Burke P, Williams D, Slater K . Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. Biochemistry. 1994; 33(48):14369-77. DOI: 10.1021/bi00252a001. View

Devanathan S, Pacheco A, Ujj L, Cusanovich M, Tollin G, Lin S . Femtosecond spectroscopic observations of initial intermediates in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila. Biophys J. 1999; 77(2):1017-23. PMC: 1300392. DOI: 10.1016/S0006-3495(99)76952-3. View

Mihara K, Hisatomi O, Imamoto Y, Kataoka M, Tokunaga F . Functional expression and site-directed mutagenesis of photoactive yellow protein. J Biochem. 1997; 121(5):876-80. DOI: 10.1093/oxfordjournals.jbchem.a021668. View

Meyer T, Yakali E, Cusanovich M, Tollin G . Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry. 1987; 26(2):418-23. DOI: 10.1021/bi00376a012. View

10.

Jiang Z, Swem L, Rushing B, Devanathan S, Tollin G, Bauer C . Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes. Science. 1999; 285(5426):406-9. DOI: 10.1126/science.285.5426.406. View

11.

Meyer T, Tollin G, Causgrove T, Cheng P, Blankenship R . Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila. Biophys J. 2009; 59(5):988-91. PMC: 1281333. DOI: 10.1016/S0006-3495(91)82313-X. View

12.

Sprenger W, Hoff W, Armitage J, Hellingwerf K . The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein. J Bacteriol. 1993; 175(10):3096-104. PMC: 204631. DOI: 10.1128/jb.175.10.3096-3104.1993. View

13.

Genick U, Soltis S, Kuhn P, Canestrelli I, Getzoff E . Structure at 0.85 A resolution of an early protein photocycle intermediate. Nature. 1998; 392(6672):206-9. DOI: 10.1038/32462. View

14.

PERMAN B, Srajer V, Ren Z, Teng T, Pradervand C, Ursby T . Energy transduction on the nanosecond time scale: early structural events in a xanthopsin photocycle. Science. 1998; 279(5358):1946-50. DOI: 10.1126/science.279.5358.1946. View

15.

Genick U, Devanathan S, Meyer T, Canestrelli I, Williams E, Cusanovich M . Active site mutants implicate key residues for control of color and light cycle kinetics of photoactive yellow protein. Biochemistry. 1997; 36(1):8-14. DOI: 10.1021/bi9622884. View

16.

Borgstahl G, Williams D, Getzoff E . 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry. 1995; 34(19):6278-87. DOI: 10.1021/bi00019a004. View

17.

van Brederode M, Gensch T, Hoff W, Hellingwerf K, Braslavsky S . Photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from Ectothiorhodospira halophila. Biophys J. 1995; 68(3):1101-9. PMC: 1281832. DOI: 10.1016/S0006-3495(95)80284-5. View

18.

Meyer T . Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim Biophys Acta. 1985; 806(1):175-83. DOI: 10.1016/0005-2728(85)90094-5. View