Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb.

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Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb. / Tveen Jensen, Karina; Strambini, G; Gonnelli, M; Broos, J; Jackson, John.

In: Biophysical Journal, Vol. 95, No. 7, 01.10.2008, p. 3419-28.

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@article{5353e9962a7c442f87007067283c57b2,
title = "Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb.",
abstract = "The dI component of Rhodospirillum rubrum transhydrogenase has a single Trp residue (Trp(72)), which has distinctive optical properties, including short-wavelength fluorescence emission with clear vibrational fine structure, and long-lived, well-resolved phosphorescence emission. We have made a set of mutant dI proteins in which residues contacting Trp(72) are conservatively substituted. The room-temperature fluorescence-emission spectra of our three Met(97) mutants are blue shifted by approximately 4 nm, giving them a shorter-wavelength emission than any other protein described in the literature, including azurin from Pseudomonas aeruginosa. Fluorescence spectra in low-temperature glasses show equivalent well-resolved vibrational bands in wild-type and the mutant dI proteins, and in azurin. Substitution of Met(97) in dI changes the relative intensities of some of these vibrational bands. The analysis supports the view that fluorescence from the Met(97) mutants arises predominantly from the (1)L(b) excited singlet state of Trp(72), whereas (1)L(a) is the predominant emitting state in wild-type dI. It is suggested that the sulfur atom of Met(97) promotes greater stabilization of (1)L(a) than either (1)L(b) or the ground state. The phosphorescence spectra of Met(97) mutants are also blue-shifted, indicating that the sulfur atom decreases the transition energy between the (3)L(a) state of the Trp and the ground state.",
author = "{Tveen Jensen}, Karina and G Strambini and M Gonnelli and J Broos and John Jackson",
year = "2008",
month = oct
day = "1",
doi = "10.1529/biophysj.108.134650",
language = "English",
volume = "95",
pages = "3419--28",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "7",

}

RIS

TY - JOUR

T1 - Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb.

AU - Tveen Jensen, Karina

AU - Strambini, G

AU - Gonnelli, M

AU - Broos, J

AU - Jackson, John

PY - 2008/10/1

Y1 - 2008/10/1

N2 - The dI component of Rhodospirillum rubrum transhydrogenase has a single Trp residue (Trp(72)), which has distinctive optical properties, including short-wavelength fluorescence emission with clear vibrational fine structure, and long-lived, well-resolved phosphorescence emission. We have made a set of mutant dI proteins in which residues contacting Trp(72) are conservatively substituted. The room-temperature fluorescence-emission spectra of our three Met(97) mutants are blue shifted by approximately 4 nm, giving them a shorter-wavelength emission than any other protein described in the literature, including azurin from Pseudomonas aeruginosa. Fluorescence spectra in low-temperature glasses show equivalent well-resolved vibrational bands in wild-type and the mutant dI proteins, and in azurin. Substitution of Met(97) in dI changes the relative intensities of some of these vibrational bands. The analysis supports the view that fluorescence from the Met(97) mutants arises predominantly from the (1)L(b) excited singlet state of Trp(72), whereas (1)L(a) is the predominant emitting state in wild-type dI. It is suggested that the sulfur atom of Met(97) promotes greater stabilization of (1)L(a) than either (1)L(b) or the ground state. The phosphorescence spectra of Met(97) mutants are also blue-shifted, indicating that the sulfur atom decreases the transition energy between the (3)L(a) state of the Trp and the ground state.

AB - The dI component of Rhodospirillum rubrum transhydrogenase has a single Trp residue (Trp(72)), which has distinctive optical properties, including short-wavelength fluorescence emission with clear vibrational fine structure, and long-lived, well-resolved phosphorescence emission. We have made a set of mutant dI proteins in which residues contacting Trp(72) are conservatively substituted. The room-temperature fluorescence-emission spectra of our three Met(97) mutants are blue shifted by approximately 4 nm, giving them a shorter-wavelength emission than any other protein described in the literature, including azurin from Pseudomonas aeruginosa. Fluorescence spectra in low-temperature glasses show equivalent well-resolved vibrational bands in wild-type and the mutant dI proteins, and in azurin. Substitution of Met(97) in dI changes the relative intensities of some of these vibrational bands. The analysis supports the view that fluorescence from the Met(97) mutants arises predominantly from the (1)L(b) excited singlet state of Trp(72), whereas (1)L(a) is the predominant emitting state in wild-type dI. It is suggested that the sulfur atom of Met(97) promotes greater stabilization of (1)L(a) than either (1)L(b) or the ground state. The phosphorescence spectra of Met(97) mutants are also blue-shifted, indicating that the sulfur atom decreases the transition energy between the (3)L(a) state of the Trp and the ground state.

U2 - 10.1529/biophysj.108.134650

DO - 10.1529/biophysj.108.134650

M3 - Article

C2 - 18599622

VL - 95

SP - 3419

EP - 3428

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 7

ER -