ArticleBiochemistry2010
Structure and ligand binding properties of the epoxidase component of styrene monooxygenase .
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 80 citations in OpenAlex.
- Biodegradation of Polystyrene byInternational journal of molecular sciences · 2024Article
- Asymmetric azidohydroxylation of styrene derivatives mediated by a biomimetic styrene monooxygenase enzymatic cascade.Catalysis science & technology · 2021Article
- Asymmetric Epoxidation and Sulfoxidation Catalyzed by a New Styrene Monooxygenase from Bradyrhizobium.Applied biochemistry and biotechnology · 2021Article
- Asp305Gly mutation improved the activity and stability of the styrene monooxygenase for efficient epoxide production in Pseudomonas putida KT2440.Microbial cell factories · 2019Article
- Structure and inhibition mechanism of the catalytic domain of human squalene epoxidase.Nature communications · 2019Article
- Loss of Function in Zeaxanthin Epoxidase ofMarine drugs · 2018Article
- Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.Biology · 2018Review
- VpStyA1/VpStyA2B of Variovorax paradoxus EPS: An Aryl Alkyl Sulfoxidase Rather than a Styrene Epoxidizing Monooxygenase.Molecules (Basel, Switzerland) · 2018Article
- A Review: The Styrene Metabolizing Cascade of Side-Chain Oxygenation as Biotechnological Basis to Gain Various Valuable Compounds.Frontiers in microbiology · 2018Review
- Chopping and Changing: the Evolution of the Flavin-dependent Monooxygenases.Journal of molecular biology · 2016Article
- Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding.AMB Express · 2015Article
- Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications.Frontiers in microbiology · 2014Review
- FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase.FEBS letters · 2013Article
- Structure and mechanism of styrene monooxygenase reductase: new insight into the FAD-transfer reaction.Biochemistry · 2013Article
- Characterization of a self-sufficient trans-anethole oxygenase from Pseudomonas putida JYR-1.PloS one · 2013Article
- Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.International journal of molecular sciences · 2012Review
- Isolation of a gene responsible for the oxidation of trans-anethole to para-anisaldehyde by Pseudomonas putida JYR-1 and its expression in Escherichia coli.Applied and environmental microbiology · 2012Article
- Enzymatic chemistry of cyclopropane, epoxide, and aziridine biosynthesis.Chemical reviews · 2012Review
- Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.The Journal of biological chemistry · 2011Article
- Nature of the reaction intermediates in the flavin adenine dinucleotide-dependent epoxidation mechanism of styrene monooxygenase.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Styrene monooxygenase (SMO) is a two-component flavoprotein monooxygenase that transforms styrene to styrene oxide in the first step of the styrene catabolic and detoxification pathway of Pseudomonas putida S12. The crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains. The overall architecture is most similar to that of p-hydroxybenzoate hydroxylase (PHBH), although there are some significant differences in secondary structure. Structural comparisons suggest that a large cavity open to the surface forms the FAD binding site. At the base of this pocket is another cavity that likely represents the styrene binding site. Flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA approximately 8000 times more tightly than the oxidized coenzyme. Equilibrium fluorescence and isothermal titration calorimetry data using benzene as a substrate analogue indicate that the oxidized flavin and substrate analogue binding equilibria of NSMOA are linked such that the binding affinity of each is increased by 60-fold when the enzyme is saturated with the other. A much weaker approximately 2-fold positive cooperative interaction is observed for the linked binding equilibria of benzene and reduced FAD. The low affinity of the substrate analogue for the reduced FAD complex of NSMOA is consistent with a preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene, identifying the apoenzyme structure as the key catalytic resting state of NSMOA poised to bind reduced FAD and initiate the oxygen reaction.
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