Electronic interactions between iron and the bound semiquinones in bacterial photosynthesis. EPR spectroscopy of oriented cells of Rhodopseudomonas viridis

G Charles Dismukes, Harry A. Frank, Richard Friesner, Kenneth Sauer

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Electron paramagnetic resonance (EPR) spectroscopy of the iron-semiquinone complex in photosynthetic bacterial cells and chromatophores of Rhodopseudomonas viridis is reported. Magnetic fields are used to orient the prolate ellipsoidal-shaped cells which possess a highly ordered internal structure, consisting of concentric, nearly cylindrical membranes. The field-oriented suspension of cells exhibits a highly dichroic EPR signal for the iron-semiquinone complex, showing that the iron possesses a low-symmetry ligand field and exists in a preferred orientation within the native reaction-center membrane complex. The EPR spectrum is analyzed utilizing a spin hamiltonian formalism to extract physical information describing the electronic structure of the iron and the nature of its interaction with the semiquinones. Exact numerical solutions and analytical expressions for the transition frequencies and intensities derived from a perturbation theory expansion are presented, and a computer-simulated spectrum is given. It has been found that, for a model which assumes no preferred orientation within the plane of the membranes, the orientation of the Fe2+ ligand axis of largest zero-field splitting (Z, the principal magnetic axis) is titled 64±6° from the membrane normal. The ligand field for Fe2+ has low symmetry, with zero-field splitting parameters of |D1|=7.0±1.3 cm-1 and |E1|=1.7±0.5 cm-1 and

Original languageEnglish
Pages (from-to)253-271
Number of pages19
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume764
Issue number3
DOIs
Publication statusPublished - Mar 30 1984

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Rhodopseudomonas
Photosynthesis
Electron Spin Resonance Spectroscopy
Paramagnetic resonance
Spectrum Analysis
Iron
Spectroscopy
Membranes
Ligands
Bacterial Chromatophores
Phosmet
Photosynthetic Reaction Center Complex Proteins
Hamiltonians
Magnetic Fields
Electronic structure
Suspensions
Magnetic fields

Keywords

  • (Rps. viridis)
  • Bacterial photosynthesis
  • Electron transport
  • ESR
  • Iron - semiquinone

ASJC Scopus subject areas

  • Biophysics

Cite this

Electronic interactions between iron and the bound semiquinones in bacterial photosynthesis. EPR spectroscopy of oriented cells of Rhodopseudomonas viridis. / Dismukes, G Charles; Frank, Harry A.; Friesner, Richard; Sauer, Kenneth.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 764, No. 3, 30.03.1984, p. 253-271.

Research output: Contribution to journalArticle

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AB - Electron paramagnetic resonance (EPR) spectroscopy of the iron-semiquinone complex in photosynthetic bacterial cells and chromatophores of Rhodopseudomonas viridis is reported. Magnetic fields are used to orient the prolate ellipsoidal-shaped cells which possess a highly ordered internal structure, consisting of concentric, nearly cylindrical membranes. The field-oriented suspension of cells exhibits a highly dichroic EPR signal for the iron-semiquinone complex, showing that the iron possesses a low-symmetry ligand field and exists in a preferred orientation within the native reaction-center membrane complex. The EPR spectrum is analyzed utilizing a spin hamiltonian formalism to extract physical information describing the electronic structure of the iron and the nature of its interaction with the semiquinones. Exact numerical solutions and analytical expressions for the transition frequencies and intensities derived from a perturbation theory expansion are presented, and a computer-simulated spectrum is given. It has been found that, for a model which assumes no preferred orientation within the plane of the membranes, the orientation of the Fe2+ ligand axis of largest zero-field splitting (Z, the principal magnetic axis) is titled 64±6° from the membrane normal. The ligand field for Fe2+ has low symmetry, with zero-field splitting parameters of |D1|=7.0±1.3 cm-1 and |E1|=1.7±0.5 cm-1 and

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