Abstract
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Catalysis
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Chemical Phenomena
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Chemistry, Physical
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Crystallization
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Crystallography, X-Ray
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Dioxygenases
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Hydroxylation
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Indoles / metabolism
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Iron / chemistry
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Iron / metabolism*
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Models, Chemical
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Models, Molecular
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Molecular Structure
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Multienzyme Complexes / chemistry*
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Multienzyme Complexes / metabolism*
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Naphthalenes
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Oxidation-Reduction
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Oxygen / chemistry
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Oxygen / metabolism*
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Oxygenases / chemistry*
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Oxygenases / metabolism*
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Protein Conformation
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Protons
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Pseudomonas / enzymology
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Stereoisomerism
Substances
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Indoles
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Multienzyme Complexes
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Naphthalenes
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Protons
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naphthalene
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indole
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Iron
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Oxygenases
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Dioxygenases
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naphthalene dioxygenase
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Oxygen