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Oxidative Decarboxylase UndA Utilizes a Dinuclear Iron Cofactor
- Source :
- Journal of the American Chemical Society. 141:8684-8688
- Publication Year :
- 2019
- Publisher :
- American Chemical Society (ACS), 2019.
-
Abstract
- UndA is a nonheme iron enzyme that activates oxygen to catalyze the decarboxylation of dodecanoic acid to undecene and carbon dioxide. We report the first optical and Mössbauer spectroscopic characterization of UndA, revealing that the enzyme harbors a coupled dinuclear iron cluster. Single turnover studies confirm that the reaction of the diferrous enzyme with dioxygen produces stoichiometric product per cluster. UndA is the first characterized example of a diiron decarboxylase, thus expanding the repertoire of reactions catalyzed by dinuclear iron enzymes.
- Subjects :
- Models, Molecular
Carboxy-Lyases
Protein Conformation
Decarboxylation
Stereochemistry
Iron
Coenzymes
chemistry.chemical_element
Oxidative phosphorylation
010402 general chemistry
01 natural sciences
Biochemistry
Oxygen
Catalysis
Cofactor
Colloid and Surface Chemistry
Unda
chemistry.chemical_classification
biology
Chemistry
General Chemistry
biology.organism_classification
0104 chemical sciences
Enzyme
biology.protein
Oxidation-Reduction
Stoichiometry
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 141
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....4d17e2db22d47e98c8fb315ca31b867a