ArticleJournal of the American Chemical Society2008
Near-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 47 citations in OpenAlex.
- Spectroscopy and crystallography define carotenoid oxygenases as a new subclass of mononuclear non-heme FeThe Journal of biological chemistry · 2025Article
- Understanding the stability of a plastic-degrading Rieske iron oxidoreductase system.Protein science : a publication of the Protein Society · 2024Article
- Custom tuning of Rieske oxygenase reactivity.Nature communications · 2023Article
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- Elucidating the Role of OACS environmental Au · 2022Article
- Substrate-Specific Coupling of OACS catalysis · 2022Article
- Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Apparently Unreactive Substrate Facilitates the Electron Transfer for Dioxygen Activation in Rieske Dioxygenases.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Design principles for site-selective hydroxylation by a Rieske oxygenase.Nature communications · 2022Article
- Salicylate 5-Hydroxylase: Intermediates in Aromatic Hydroxylation by a Rieske Monooxygenase.Biochemistry · 2019Article
- Geometric and Electronic Structural Contributions to Fe/OBulletin of Japan Society of Coordination Chemistry · 2019Article
- Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.Applied microbiology and biotechnology · 2018Review
- NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native FeJournal of the American Chemical Society · 2018Article
- Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center.Biochemistry · 2017Article
- Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.Chemical science · 2017Article
- OBiochemistry · 2016Article
- Rate-Determining Attack on Substrate Precedes Rieske Cluster Oxidation during Cis-Dihydroxylation by Benzoate Dioxygenase.Biochemistry · 2015Article
- The role of chloride in the mechanism of O(2) activation at the mononuclear nonheme Fe(II) center of the halogenase HctB.Journal of the American Chemical Society · 2014Article
- Molecular Dynamics Simulation of Nitrobenzene Dioxygenase Using AMBER Force Field.Journal of chemical theory and computation · 2014Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
Near-IR MCD and variable temperature, variable field (VTVH) MCD have been applied to naphthalene 1,2-dioxygenase (NDO) to describe the coordination geometry and electronic structure of the mononuclear nonheme ferrous catalytic site in the resting and substrate-bound forms with the Rieske 2Fe2S cluster oxidized and reduced. The structural results are correlated with the crystallographic studies of NDO and other related Rieske nonheme iron oxygenases to develop molecular level insights into the structure/function correlation for this class of enzymes. The MCD data for resting NDO with the Rieske center oxidized indicate the presence of a six-coordinate high-spin ferrous site with a weak axial ligand which becomes more tightly coordinated when the Rieske center is reduced. Binding of naphthalene to resting NDO (Rieske oxidized and reduced) converts the six-coordinate sites into five-coordinate (5c) sites with elimination of a water ligand. In the Rieske oxidized form the 5c sites are square pyramidal but transform to a 1:2 mixture of trigonal bipyramial/square pyramidal sites when the Rieske center is reduced. Thus the geometric and electronic structure of the catalytic site in the presence of substrate can be significantly affected by the redox state of the Rieske center. The catalytic ferrous site is primed for the O2 reaction when substrate is bound in the active site in the presence of the reduced Rieske site. These structural changes ensure that two electrons and the substrate are present before the binding and activation of O2, which avoids the uncontrolled formation and release of reactive oxygen species.
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