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Gentisate 1,2-dioxygenase from Pseudomonas. Substrate coordination to active site Fe
2+
and mechanism of turnover
M. R. Harpel, J. D. Lipscomb
Biochemistry, Molecular Biology, and Biophysics (TMED)
Research output
:
Contribution to journal
›
Article
›
peer-review
81
Scopus citations
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Dive into the research topics of 'Gentisate 1,2-dioxygenase from Pseudomonas. Substrate coordination to active site Fe
2+
and mechanism of turnover'. Together they form a unique fingerprint.
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Chemistry
Iron
100%
Dioxygenases
100%
Carbon
66%
Water Type
33%
Hydroxyl
33%
Group
25%
EPR Spectroscopy
25%
Ligand
16%
Spectra
16%
Aromatic Structure
16%
Ring Cleavage
16%
Electron Particle
8%
Atom
8%
Rate
8%
Catalysis
8%
Chemical Reaction Product
8%
Chemical Reaction
8%
Amine
8%
Heme
8%
Chemical Kinetics Characteristics
8%
Dioxygen
8%
Chemical Bond
8%
Cleavage
8%
Resonance
8%
Hydroxyl Group
8%
Reaction Stoichiometry
8%
Biochemistry, Genetics and Molecular Biology
Active Site
100%
Dioxygenase
100%
Coordination
100%
Pseudomonas
100%
Lysozyme
41%
Spectrum
16%
Electron
8%
Position
8%
Association
8%
Catalysis
8%
Atom
8%
Stoichiometry
8%
Chemical Reaction Kinetics
8%
Comamonas testosteroni
8%
Delftia acidovorans
8%