Ultrafast photoreactions in protein nanospaces as revealed by fs fluorescence dynamics measurements on photoactive yellow protein and related systemsDedicated to Professor Dr Z. R. Grabowski and Professor Dr J. Wirz on the occasions of their 75th and 60th birthdays.

Mataga, Noboru; Chosrowjan, Haik; Taniguchi, Seiji; Hamada, Norio; Tokunaga, Fumio; Imamoto, Yasushi; Kataoka, Mikio

doi:10.1039/b212699k

Cited by 54 publications

(56 citation statements)

References 19 publications

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“…The dynamics is dominated by solvation effect. 11) Three exponential model function with a rise component was sufficient to reproduce accurately the dynamics in this case. Our analysis shows that the initial phases of the oscillatory modes in proteins depend on observation wavelength and a phase shift of π from "blue" to "red" is clearly observed for both modes.…”

Section: "Time Domain" Investigationsmentioning

confidence: 94%

“…Additional details of these observations have been summarized in recent articles by Mataga et al. 10,11) Briefly, for intact proteins, the fluorescence decay curves with coupled oscillations can be well reproduced by double exponential decays superimposed with exponentially damping two oscillatory modes. On the other hand, for denatured PYP no oscillations in fluorescence decays have been observed.…”

Section: "Time Domain" Investigationsmentioning

confidence: 95%

“…Our analysis shows that the initial phases of the oscillatory modes in proteins depend on observation wavelength and a phase shift of π from "blue" to "red" is clearly observed for both modes. 11) Hence, the observed oscillations could be explained by the transition frequency modulation mechanism. Further evidence supporting this mechanism is the fact that the amplitudes of vibrations are rather small at the maximum compared with that at the blue and red edges of the fluorescence spectrum.…”

Section: "Time Domain" Investigationsmentioning

confidence: 99%

“…With improved time resolution of the apparatus we have actually observed such oscillations recently. 6,11) However, the origin and role of the low frequency intraprotein vibrations in the early ultrafast events of PYP is not very clear yet. Following simple considerations emphasize their potential importance.…”

Section: Introductionmentioning

confidence: 99%

“…3) Using results of diverse experimental studies 3,6,11,14) and quantum mechanical calculations 13) it was demonstrated that PYP's photocycle is initiated by flipping the carbonyl group of its chromophore (pcoumaric acid) rather than its bulky aromatic ring. This result implies that the chromophore isomerization requires only minor rearrangements of the chromophore/protein structures in protein nanospace (PNS) during the initial ultrafast events.…”

Section: Introductionmentioning

confidence: 99%

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Time and Frequency Domain Investigations on Ultrafast Photoreaction Dynamics of Photoactive Yellow Protein (PYP)

Chosrowjan

Mataga

Taniguchi

et al. 2004

The Review of Laser Engineering

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Low frequency vibrations of the native PYP and related systems in solution have been investigated in "time" (fs fluorescence up-conversion) and "frequency" (resonance Raman) domains to elucidate their role in ultrafast photoisomerization reaction dynamics of PYP. Tentative assignments of the oscillatory components to particular vibrations are proposed supported by normal mode calculations based on DFT and ab initio MO methods. It is concluded that the out-of-plane skeleton bending mode of the chromophore, γ 16 , is responsible for the observed oscillations in native and all mutant PYPs (f 1 ~ 135 cm -1 ), while in-plane ν' 42 and ν' 43 modes are probably responsible for oscillations observed in the PYP analogue with locked chromophore. A dynamic model called "trigger mode mediated guidance" has been proposed to explain in simple terms the ultrafast primary process initiating PYP's photocycle. Furthermore, first successful fluorescence dynamics experiments on PYP single crystals with femtosecond time resolution are presented and discussed.

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Section: "Time Domain" Investigationsmentioning

confidence: 94%

Section: "Time Domain" Investigationsmentioning

confidence: 95%

Section: "Time Domain" Investigationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Time and Frequency Domain Investigations on Ultrafast Photoreaction Dynamics of Photoactive Yellow Protein (PYP)

Chosrowjan

Mataga

Taniguchi

et al. 2004

The Review of Laser Engineering

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Photoactive Yellow Protein, the Xanthopsin

Horst

Hendriks

Vreede

et al. 2005

Handbook of Photosensory Receptors

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Changes in Active Site Hydrogen Bonding upon Formation of the Electronically Excited State of Photoactive Yellow Protein

Hoff

Kang

Kumauchi

et al. 2010

Hydrogen Bonding and Transfer in the Excited State

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Light plays three main roles in biology. First, light from the sun provides the main source of energy driving the biosphere through chlorophyll-based electron transfer in photosynthetic reaction centers and retinal-based proton pumping in rhodopsins [1]. Second, light is a source of information about the environment for many organisms using photosensory proteins, including animals, plants, fungi and bacteria [2,3]. Third, light can cause damage to biological systems. Light from the near-UV region can damage DNA [4], and excess visible light can damage the photosynthetic machinery in photoinhibition [5]. Thus, light is of great importance for a wide range of biological processes.Proteins that perform photosynthesis or light sensing consist of an apoprotein and a bound chromophore. Only a small number of chromophores account for most known processes in photobiology: chlorophyll and linear tetrapyrroles, caretoids and retinal, flavins and p-coumaric acid [2]. In many cases the chromophore has strong and functionally important interactions with the protein binding pocket, particularly charge-charge interactions and hydrogen bonding interactions. While many different proteins interact with light in a wide range of organisms, almost all of these systems are based on key types of photochemical processes, including electron transfer, C¼C double bond isomerization and the formation of chemical bonds [2,6]. These photochemical events often trigger a cascade of thermal reactions in the protein that extends to the millisecond and minute range, and that result in a biologically relevant output. If the cascade of thermal reactions results in the re-formation of the initial state, the process is referred to as a photocycle. It is the initial ultrafast

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Ultrafast photoreactions in protein nanospaces as revealed by fs fluorescence dynamics measurements on photoactive yellow protein and related systemsDedicated to Professor Dr Z. R. Grabowski and Professor Dr J. Wirz on the occasions of their 75th and 60th birthdays.

Cited by 54 publications

References 19 publications

Time and Frequency Domain Investigations on Ultrafast Photoreaction Dynamics of Photoactive Yellow Protein (PYP)

Time and Frequency Domain Investigations on Ultrafast Photoreaction Dynamics of Photoactive Yellow Protein (PYP)

Photoactive Yellow Protein, the Xanthopsin

Changes in Active Site Hydrogen Bonding upon Formation of the Electronically Excited State of Photoactive Yellow Protein

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