High-field Mössbauer studies of reduced protocatechuate 3,4-dioxygenase

R. Zimmermann, B. H. Huynh, E. Münck, John D Lipscomb

Research output: Contribution to journalArticle

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Abstract

We have studied the Mössbauer spectra of reduced protocatechuate 3,4-dioxygenase (3,4-PCase) from P. aeruginosa in the temperature range from 1.5 to 200 K in applied magnetic fields up to 55 kG. The entire data set was fitted to a spin Hamiltonian pertinent to the high-spin ferrous ion. By judiciously choosing the experimental conditions, the multiparameter problem could be solved rather unambiguously. The iron sites of reduced 3,4-PCase are characterized by a negative zero-field splitting parameter D = -(6±1) cm-1 and a large rhombicity E/D = 0.25±0.05. The data show clearly that the electric field gradient tensor is rotated relative to the zero-field splitting, suggesting a point symmetry of monoclinic or lower. The electronic spin relaxation rate, at 4.2 K, is slower than 107 s-1.

Original languageEnglish (US)
Pages (from-to)5463-5467
Number of pages5
JournalThe Journal of chemical physics
Volume69
Issue number12
DOIs
StatePublished - Jan 1 1978

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Protocatechuate-3,4-Dioxygenase
Hamiltonians
Tensors
Iron
Electric fields
Ions
Magnetic fields
Temperature
tensors
iron
gradients
electric fields
symmetry
electronics
magnetic fields
ions
temperature

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High-field Mössbauer studies of reduced protocatechuate 3,4-dioxygenase. / Zimmermann, R.; Huynh, B. H.; Münck, E.; Lipscomb, John D.

In: The Journal of chemical physics, Vol. 69, No. 12, 01.01.1978, p. 5463-5467.

Research output: Contribution to journalArticle

Zimmermann, R. ; Huynh, B. H. ; Münck, E. ; Lipscomb, John D. / High-field Mössbauer studies of reduced protocatechuate 3,4-dioxygenase. In: The Journal of chemical physics. 1978 ; Vol. 69, No. 12. pp. 5463-5467.
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