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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
82
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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Biochemistry, Genetics and Molecular Biology
Active Site
100%
Association
16%
Atom
16%
Catalysis
16%
Chemical Reaction Kinetics
16%
Comamonas testosteroni
16%
Coordination
100%
Delftia acidovorans
16%
Dioxygenase
100%
Electron
16%
Iron
100%
Lysozyme
83%
Position
16%
Pseudomonas
100%
Spectrum
33%
Stoichiometry
16%
Chemistry
2,5-dihydroxybenzoate
12%
Amine
12%
Aromatic Structure
25%
Atom
12%
Carbon
100%
Catalysis
12%
Chemical Bond
12%
Chemical Kinetics Characteristics
12%
Chemical Reaction
12%
Chemical Reaction Product
12%
Dioxygen
12%
Electron Particle
12%
EPR Spectroscopy
37%
Group
37%
Heme
12%
Hydroxyl
50%
Hydroxyl Group
12%
Ligand
25%
Rate
12%
Reaction Stoichiometry
12%
Ring Cleavage
25%
Spectra
25%
Water Type
50%