Protocatechuate 3,4-dioxygenase. Resonance Raman studies of the oxygenated intermediate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference25 articles.
1. Nonidentical subunits of protocatechuate 3,4-dioxygenase
2. Mössbauer and EPR spectroscopy on protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa
3. Protocatechuate 3,4-dioxygenase
4. Resonance Raman spectra of protocatechuate 3,4-dioxygenase. Evidence for coordination of tyrosine residue to ferric iron
5. Raman spectral evidence for tyrosine coordination of iron in protocatechuate 3,4-dioxygenase
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2. Analogues of the iron-binding site in catechol 1,2-dioxygenase: iron(III) complexes of benzimidazole and pyridine-containing tridentate ligands;Journal of the Chemical Society, Dalton Transactions;1995
3. Evidence for retention of biological activity of a non-heme iron enzyme adsorbed on a silver colloid: A surface-enhanced resonance Raman scattering study;Biochemistry;1993-12-01
4. Catalytic Oxidation of Catechols;Catalysis by Metal Complexes;1992
5. Interaction of the iron(III) complex of N-[2-((o-Hydroxyphenyl)glycino)ethyl]salicylideneamine with catechol and cyanide: a model for the binding site in the dioxygenase enzymes;Inorganic Chemistry;1989-01
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