An LD-ADMR study on reaction centers of the LH(L131) and LH(M160) hydrogen-bonding mutants of Rhodobacter sphaeroides

J. Vrieze, J. C. Williams, James Paul Allen, A. J. Hoff

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Reaction centers of the LH(L131) and LH(M160) mutants of Rhodobacter sphaeroides, which have a leucine near the primary donor, a bacteriochlorophyll dimer, changed into a histidine, have been investigated with linear-dichroic absorbance-detected magnetic resonance, and the results are compared with those obtained for native reaction centers. The microwave-induced triplet-minus-singlet absorbance-difference spectra of the three reaction centers upon triplet formation of the primary donor show small differences in band shifts in the Q(Y)-region of the accessory bacteriochrorophylls. The orientations of the Q(Y)-transition moments with respect to the dipolar axes of the triplet state of the primary donor were found to be equal for all reaction centers, indicating that the orientation of the triplet axes with respect to the reaction center coordinate frame is the same for all three reaction centers. From this we conclude that the electronic composition of the triplet state and the Q(Y) transitions are basically the same for the mutant and native reaction centers.

Original languageEnglish
Pages (from-to)221-228
Number of pages8
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1276
Issue number3
DOIs
Publication statusPublished - Sep 30 1996

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Bacteriochlorophylls
Rhodobacter sphaeroides
Accessories
Magnetic resonance
Hydrogen Bonding
Microwaves
Histidine
Leucine
Dimers
Hydrogen bonds
Magnetic Resonance Spectroscopy
Chemical analysis

Keywords

  • Absorbance-detected magnetic resonance
  • Bacterial reaction center
  • Mutant
  • Photosynthesis
  • Triplet state

ASJC Scopus subject areas

  • Biophysics

Cite this

An LD-ADMR study on reaction centers of the LH(L131) and LH(M160) hydrogen-bonding mutants of Rhodobacter sphaeroides. / Vrieze, J.; Williams, J. C.; Allen, James Paul; Hoff, A. J.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1276, No. 3, 30.09.1996, p. 221-228.

Research output: Contribution to journalArticle

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AU - Hoff, A. J.

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N2 - Reaction centers of the LH(L131) and LH(M160) mutants of Rhodobacter sphaeroides, which have a leucine near the primary donor, a bacteriochlorophyll dimer, changed into a histidine, have been investigated with linear-dichroic absorbance-detected magnetic resonance, and the results are compared with those obtained for native reaction centers. The microwave-induced triplet-minus-singlet absorbance-difference spectra of the three reaction centers upon triplet formation of the primary donor show small differences in band shifts in the Q(Y)-region of the accessory bacteriochrorophylls. The orientations of the Q(Y)-transition moments with respect to the dipolar axes of the triplet state of the primary donor were found to be equal for all reaction centers, indicating that the orientation of the triplet axes with respect to the reaction center coordinate frame is the same for all three reaction centers. From this we conclude that the electronic composition of the triplet state and the Q(Y) transitions are basically the same for the mutant and native reaction centers.

AB - Reaction centers of the LH(L131) and LH(M160) mutants of Rhodobacter sphaeroides, which have a leucine near the primary donor, a bacteriochlorophyll dimer, changed into a histidine, have been investigated with linear-dichroic absorbance-detected magnetic resonance, and the results are compared with those obtained for native reaction centers. The microwave-induced triplet-minus-singlet absorbance-difference spectra of the three reaction centers upon triplet formation of the primary donor show small differences in band shifts in the Q(Y)-region of the accessory bacteriochrorophylls. The orientations of the Q(Y)-transition moments with respect to the dipolar axes of the triplet state of the primary donor were found to be equal for all reaction centers, indicating that the orientation of the triplet axes with respect to the reaction center coordinate frame is the same for all three reaction centers. From this we conclude that the electronic composition of the triplet state and the Q(Y) transitions are basically the same for the mutant and native reaction centers.

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