Pigment-Protein Interactions in Phytochromes Probed by Fluorescence Line Narrowing Spectroscopy

J.B. Nieder; E.A Stojkovic; K. Moffat; K.T. Forest; T. Lamparter; R. Bittl; J.T.M. Kennis

doi:10.1021/jp409110q

Pigment-Protein Interactions in Phytochromes Probed by Fluorescence Line Narrowing Spectroscopy

J.B. Nieder, E.A Stojkovic, K. Moffat, K.T. Forest, T. Lamparter, R. Bittl, J.T.M. Kennis

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Fluorescence line narrowing (FLN) spectroscopy was used to study bacteriophytochromes and variants from various species in their red-absorbing Pr ground state, including phytochromes Agp1 from Agrobacterium tumefaciens, DrBphP from Deinococcus radiodurans, and RpBphP2 and RpBphP3 from Rhodopseudomonas palustris. A species-dependent narrowing of the fluorescence emission bands is observed. The results suggest varied pigment-protein interactions, possibly connected to chromophore mobility or extended water pyrrole networks inside of the differing binding pockets. Solvent water isotope exchange from H

Original language	English
Pages (from-to)	14940-14950
Journal	Journal of Physical Chemistry B
Volume	117
Issue number	48
DOIs	https://doi.org/10.1021/jp409110q
Publication status	Published - 2013

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1021/jp409110q

Handle.net

Persistent link

Cite this

@article{cf421a6d77274c579048a29e0db11e26,

title = "Pigment-Protein Interactions in Phytochromes Probed by Fluorescence Line Narrowing Spectroscopy",

abstract = "Fluorescence line narrowing (FLN) spectroscopy was used to study bacteriophytochromes and variants from various species in their red-absorbing Pr ground state, including phytochromes Agp1 from Agrobacterium tumefaciens, DrBphP from Deinococcus radiodurans, and RpBphP2 and RpBphP3 from Rhodopseudomonas palustris. A species-dependent narrowing of the fluorescence emission bands is observed. The results suggest varied pigment-protein interactions, possibly connected to chromophore mobility or extended water pyrrole networks inside of the differing binding pockets. Solvent water isotope exchange from H",

author = "J.B. Nieder and E.A Stojkovic and K. Moffat and K.T. Forest and T. Lamparter and R. Bittl and J.T.M. Kennis",

year = "2013",

doi = "10.1021/jp409110q",

language = "English",

volume = "117",

pages = "14940--14950",

journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

publisher = "American Chemical Society",

number = "48",

}

TY - JOUR

T1 - Pigment-Protein Interactions in Phytochromes Probed by Fluorescence Line Narrowing Spectroscopy

AU - Nieder, J.B.

AU - Stojkovic, E.A

AU - Moffat, K.

AU - Forest, K.T.

AU - Lamparter, T.

AU - Bittl, R.

AU - Kennis, J.T.M.

PY - 2013

Y1 - 2013

N2 - Fluorescence line narrowing (FLN) spectroscopy was used to study bacteriophytochromes and variants from various species in their red-absorbing Pr ground state, including phytochromes Agp1 from Agrobacterium tumefaciens, DrBphP from Deinococcus radiodurans, and RpBphP2 and RpBphP3 from Rhodopseudomonas palustris. A species-dependent narrowing of the fluorescence emission bands is observed. The results suggest varied pigment-protein interactions, possibly connected to chromophore mobility or extended water pyrrole networks inside of the differing binding pockets. Solvent water isotope exchange from H

AB - Fluorescence line narrowing (FLN) spectroscopy was used to study bacteriophytochromes and variants from various species in their red-absorbing Pr ground state, including phytochromes Agp1 from Agrobacterium tumefaciens, DrBphP from Deinococcus radiodurans, and RpBphP2 and RpBphP3 from Rhodopseudomonas palustris. A species-dependent narrowing of the fluorescence emission bands is observed. The results suggest varied pigment-protein interactions, possibly connected to chromophore mobility or extended water pyrrole networks inside of the differing binding pockets. Solvent water isotope exchange from H

U2 - 10.1021/jp409110q

DO - 10.1021/jp409110q

M3 - Article

SN - 1520-6106

VL - 117

SP - 14940

EP - 14950

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 48

ER -

Pigment-Protein Interactions in Phytochromes Probed by Fluorescence Line Narrowing Spectroscopy

Abstract

UN SDGs

Access to Document

Handle.net

Fingerprint

Cite this