Mechanism and Catalytic Diversity of Rieske Non-Heme Iron-Dependent Oxygenases

Barry, Sarah M.; Challis, Gregory L.

doi:10.1021/cs400087p

Cited by 208 publications

(218 citation statements)

References 77 publications

Supporting

Mentioning

208

Contrasting

Unclassified

Order By: Relevance

“…Nevertheless, this viewpoint has been recently challenged, and homolytic O-O breakage and transfer of OH radical was suggested instead. 9 For Rieske-type non-heme monoiron oxygenases 10 hydroxylating aromatic rings, naphthalene dioxygenase for example, no conclusive mechanism has been obtained yet. The presence of two open cis-aligned coordination sites on the iron center allows the formation of a side-on bound Fe(III)-OOH complex, which has long been considered a key intermediate.…”

Section: Introductionmentioning

confidence: 99%

Pathways for Arene Oxidation in Non-Heme Diiron Enzymes: Lessons from Computational Studies on Benzoyl Coenzyme A Epoxidase

Rokob

2016

J. Am. Chem. Soc.

View full text Add to dashboard Cite

Oxygenation of aromatic rings using O2 is catalyzed by several non-heme carboxylate-bridged diiron enzymes. In order to provide a general mechanistic description for these reactions, computational studies were carried out at the ONIOM(B3LYP/BP86/Amber) level on the non-heme diiron enzyme benzoyl Specifically for the BoxB enzyme, the Q pathway was found to be the most preferred, but the corresponding bis(μ-oxo)-diiron(IV) species is significantly destabilized and not expected to be directly observable. Epoxidation via the Pσ* pathway represents an energetically somewhat higher lying alternative; possible strategies for experimental discrimination are discussed. The selectivity toward epoxidation is shown to stem from a combination of inherent electronic properties of the thioacyl substituent and enzymatic constraints. Possible implications of the results for toluene monooxygenases are considered as well.2

show abstract

Section: Introductionmentioning

confidence: 99%

Pathways for Arene Oxidation in Non-Heme Diiron Enzymes: Lessons from Computational Studies on Benzoyl Coenzyme A Epoxidase

Rokob

2016

J. Am. Chem. Soc.

View full text Add to dashboard Cite

show abstract

“…With these enzymes ystems it is possible to address monohydroxylations( Scheme 1, path I), dihydroxylations (Scheme 1, path II), and O-dealkylations (Scheme 1, path III) with high regio-a nd stereoselectivities. [11,12] Recently,s emirational engineering of the cumene dioxygenase (CDO) from Pseudomonas fluorescens IP01 expanded the substrate scope of these versatile catalysts to ar ange of sterically demanding cyclic and linear alkenesa nd monoterpenes. The CDOs ingle variant M232Aw as able to convert different terpeneg eometries such as myrcene and (À)-a-pinene with high specificity and selectivity.…”

mentioning

confidence: 99%

Semirational Engineering of the Naphthalene Dioxygenase from Pseudomonas sp. NCIB 9816‐4 towards Selective Asymmetric Dihydroxylation

2017

View full text Add to dashboard Cite

Enzyme-catalyzed asymmetric dihydroxylation is ap owerful tool fort he selective oxyfunctionalization of various organic compounds. By applying Rieske non-heme dioxygenases (ROs), molecular oxygen and ar eduction equivalent are needed for the generation of vicinal cis-diols. We report ac omprehensive mutagenesis study of the active site of the naphthalene dioxygenasef rom Pseudomonas sp. NCIB 9816-4 comprising 62 variants. We aimed to understand the important structure-function relationships by investigating different substituted arene substrates and the geometry of the active site. Introducing single-point mutations at positions F202, A206, V260, H295, F352, and L307 resulted in drastic shifts in the reactions pecificity,r egioselectivity,a nd stereoselectivity (! 90 %) while maintaining the residual activity towards the natural substrate naphthalene.One of the key reactions in chemistryi st he selective oxyfunctionalization of organic compounds. In this context, chiralv icinal 1,2-diols are of particular interest and are often applied as chiral ligands, auxiliaries, and chiral synthons for pharmaceuticals and agrochemicals.[1] These functionalized compounds are generated by multicomponent Rieske non-heme dioxygenases (ROs), which, analogously to some P450sm onooxygenases, consist of ar eductase, af erredoxin, andahexameric oxygenase.[2] In ROs, categorized as types III and IV,t he reductase obtains electrons from the naturalc osubstrate NAD(P)H,a nd a ferredoxin component shuttles electrons from the reductase to the oxygenase active site, at which actual oxygen activation and substrate hydroxylation occur. [3,4] Representing ab iocatalytic alternative to asymmetricd ihydroxylation with toxic transition-metal catalysts, ROs also exhibit ab road substrate scope.[5] Over 300 diverse substrates ranging from polyaromatic hydrocarbons such as phenanthracene to halogenated ethylenes and flavonoid structures were reportedt ob eh ydroxylated with these enzymes. [6,7] Furthermore, ROs were shown to be suitable for bioremediation applications and to have the ability to process xenobiotics. [8,9] In industry, ROs are utilized to manufacture the blue dye indigo, which is crucial for the production of denim cloth.[10]Oxygen-dependent ROsn ot only convert ah uge variety of compounds, but these catalysts also displayabroad reaction scope. With these enzymes ystems it is possible to address monohydroxylations( Scheme 1, path I), dihydroxylations (Scheme 1, path II), and O-dealkylations (Scheme 1, path III) with high regio-a nd stereoselectivities. [11,12] Recently,s emirational engineering of the cumene dioxygenase (CDO) from Pseudomonas fluorescens IP01 expanded the substrate scope of these versatile catalysts to ar ange of sterically demanding cyclic and linear alkenesa nd monoterpenes. The CDOs ingle variant M232Aw as able to convert different terpeneg eometries such as myrcene and (À)-a-pinene with high specificity and selectivity. [13] This work motivated us to gain furtheri nsighti nto crucial structure-function relation...

show abstract

“…In living organisms, N-dealkylation by members of the cytochrome P450 and Rieske non-heme iron oxygenase (RHO) families is an important metabolic or detoxification mechanism for many N-alkyl-containing natural or xenobiotic compounds (13)(14)(15). RHOs are characterized by utilizing Rieske-type non-heme Fe(II) as the catalytic center, and they are important enzymes for the degradation of xenobiotics and the biosynthesis of bioactive natural compounds (14,16).…”

mentioning

confidence: 99%

Novel Three-Component Rieske Non-Heme Iron Oxygenase System Catalyzing the N -Dealkylation of Chloroacetanilide Herbicides in Sphingomonads DC-6 and DC-2

Chen

Wang

Deng

et al. 2014

Appl Environ Microbiol

View full text Add to dashboard Cite

Sphingomonads DC-6 and DC-2 degrade the chloroacetanilide herbicides alachlor, acetochlor, and butachlor via N-dealkylation. In this study, we report a three-component Rieske non-heme iron oxygenase (RHO) system catalyzing the N-dealkylation of these herbicides. The oxygenase component gene cndA is located in a transposable element that is highly conserved in the two strains. CndA shares 24 to 42% amino acid sequence identities with the oxygenase components of some RHOs that catalyze N-or O-demethylation. Two putative [2Fe-2S] ferredoxin genes and one glutathione reductase (GR)-type reductase gene were retrieved from the genome of each strain. These genes were not located in the immediate vicinity of cndA. The four ferredoxins share 64 to 72% amino acid sequence identities to the ferredoxin component of dicamba O-demethylase (DMO), and the two reductases share 62 to 65% amino acid sequence identities to the reductase component of DMO. cndA, the four ferredoxin genes, and the two reductases genes were expressed in Escherichia coli, and the recombinant proteins were purified using Ni-affinity chromatography. The individual components or the components in pairs displayed no activity; the enzyme mixture showed Ndealkylase activities toward alachlor, acetochlor, and butachlor only when CndA-His 6 was combined with one of the four ferredoxins and one of the two reductases, suggesting that the enzyme consists of three components, a homo-oligomer oxygenase, a [2Fe-2S] ferredoxin, and a GR-type reductase, and CndA has a low specificity for the electron transport component (ETC). The N-dealkylase utilizes NADH, but not NADPH, as the electron donor.

show abstract

Mechanism and Catalytic Diversity of Rieske Non-Heme Iron-Dependent Oxygenases

Cited by 208 publications

References 77 publications

Pathways for Arene Oxidation in Non-Heme Diiron Enzymes: Lessons from Computational Studies on Benzoyl Coenzyme A Epoxidase

Pathways for Arene Oxidation in Non-Heme Diiron Enzymes: Lessons from Computational Studies on Benzoyl Coenzyme A Epoxidase

Semirational Engineering of the Naphthalene Dioxygenase from Pseudomonas sp. NCIB 9816‐4 towards Selective Asymmetric Dihydroxylation

Novel Three-Component Rieske Non-Heme Iron Oxygenase System Catalyzing the N -Dealkylation of Chloroacetanilide Herbicides in Sphingomonads DC-6 and DC-2

Contact Info

Product

Resources

About