ArticleBiochemistry2011
Nature of the reaction intermediates in the flavin adenine dinucleotide-dependent epoxidation mechanism of styrene monooxygenase.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 52 citations in OpenAlex.
- Enzymatic strategies for asymmetric synthesis.RSC chemical biology · 2021Review
- Asymmetric azidohydroxylation of styrene derivatives mediated by a biomimetic styrene monooxygenase enzymatic cascade.Catalysis science & technology · 2021Article
- The Sandarazols are Cryptic and Structurally Unique Plasmid-Encoded Toxins from a Rare Myxobacterium*.Angewandte Chemie (International ed. in English) · 2021Article
- Synthetic C6-Functionalized Aminoflavin Catalysts Enable Aerobic Bromination of Oxidation-Prone Substrates.Angewandte Chemie (International ed. in English) · 2020Article
- 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
- Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding.AMB Express · 2015Article
- 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
- Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.International journal of molecular sciences · 2012Review
- Enzymatic chemistry of cyclopropane, epoxide, and aziridine biosynthesis.Chemical reviews · 2012Review
- Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.The Journal of biological chemistry · 2011Article
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2 authors at 1 institution in 1 country.
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Abstract
Styrene monooxygenase (SMO) is a two-component flavoenzyme composed of an NADH-specific flavin reductase (SMOB) and FAD-specific styrene epoxidase (NSMOA). NSMOA binds tightly to reduced FAD and catalyzes the stereospecific addition of one atom of molecular oxygen to the vinyl side chain of styrene in the enantioselective synthesis of S-styrene oxide. In this mechanism, molecular oxygen first reacts with NSMOA(FAD(red)) to yield an FAD C(4a)-peroxide intermediate. This species is nonfluorescent and has an absorbance maximum of 382 nm. Styrene then reacts with the peroxide intermediate with a second-order rate constant of (2.6 ± 0.1) × 10(6) M(-1) s(-1) to yield a fluorescent intermediate with an absorbance maximum of 368 nm. We compute an activation free energy of 8.7 kcal/mol for the oxygenation step, in good agreement with that expected for a peroxide-catalyzed epoxidation, and acid-quenched samples recovered at defined time points in the single-turnover reaction indicate that styrene oxide synthesis is coincident with the formation phase of the fluorescent intermediate. These findings support FAD C(4a)-peroxide being the oxygen atom donor and the identity of the fluorescent intermediate as an FAD C(4a)-hydroxide product of the styrene epoxidation. Overall, four pH-dependent rate constants corresponding to peroxyflavin formation (pK(a) = 7.2), styrene epoxidation (pK(a) = 7.7), styrene oxide dissociation (pK(a) = 8.3), and hydroxyflavin dehydration (pK(a) = 7.6) are needed to fit the single-turnover kinetics.
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