109380-06-5

Upstream product

• 10136-84-2 Indenyl-⁽³⁾-magnesiumbromid 
• 768-22-9 2,3-dihydro-1H-indene 2,3-oxide 
• 83-33-0 inden-1-one 
• 95-13-6 1-indene 
• 20669-47-0 indenyllithium 
• 496-11-7 INDANE 
• 1452892-54-4 1-(2-vinylphenyl)prop-2-en-1-ol 
• 2039-88-5 2-bromostyrene 
• 28272-96-0 2-vinylbenzaldehyde 
• 24329-96-2 2-iodoindane 

Downstream Products

• 480-90-0 1H-inden-1-one 
• 22228-27-9 endo-Cycloprop<2,3>inden-1-ol 
• 83-33-0 inden-1-one 
• 240802-42-0 (-)-(1S,2R,3S)-1,2-Epoxy-3-hydroxyindane 
• 697-64-3 (R)-indan-1-ol 
• 61463-14-7 3,5-Dinitro-benzoic acid (1aR,6S,6aS)-(1,1a,6,6a-tetrahydro-cyclopropa[a]inden-6-yl) ester 

Relevant academic research and scientific papers

Engineering Rieske Non-Heme Iron Oxygenases for the Asymmetric Dihydroxylation of Alkenes

The asymmetric dihydroxylation of olefins is of special interest due to the facile transformation of the chiral diol products into valuable derivatives. Rieske non-heme iron oxygenases (ROs) represent promising biocatalysts for this reaction as they can be engineered to efficiently catalyze the selective mono- and dihydroxylation of various olefins. The introduction of a single point mutation improved selectivities (≥95 %) and conversions (>99 %) towards selected alkenes. By modifying the size of one active site amino acid side chain, we were able to modulate the regio- and stereoselectivity of these enzymes. For distinct substrates, mutants displayed altered regioselectivities or even favored opposite enantiomers compared to the wild-type ROs, offering a sustainable approach for the oxyfunctionalization of a wide variety of structurally different olefins. Modulation by mutation: Rieske non-heme iron oxygenases can be used as efficient biocatalysts for the selective oxyfunctionalization of various olefins yielding vicinal cis-diols and allylic alcohols. Introduction of a single amino acid substitution in the active sites of two selected oxygenases resulted in variants with improved stereoselectivities and product formations.

Stereospecific Benzylic Hydroxylation of Bicyclic Alkenes by Pseudomonas putida: Isolation of (+)-R-1-Hydroxy-1,2-dihydronaphthalene, an Arene Hydrate of Naphthalene from Metabolism of 1,2-Dihydronaphthalene

Metabolism of the bicyclic alkenes 1,2-dihydronaphthalene, indene, and 1,2-benzocyclohepta-1,3-diene by a mutant strain of Pseudomonas putida yields benzylic monols (exclusively with R configuration) as metabolites and vicinal cis diols as minor products having an excess of the S configuration at the benzylic position.

Artificial Light-Harvesting Complexes Enable Rieske Oxygenase Catalyzed Hydroxylations in Non-Photosynthetic cells

In this study, we coupled a well-established whole-cell system based on E. coli via light-harvesting complexes to Rieske oxygenase (RO)-catalyzed hydroxylations in vivo. Although these enzymes represent very promising biocatalysts, their practical applicability is hampered by their dependency on NAD(P)H as well as their multicomponent nature and intrinsic instability in cell-free systems. In order to explore the boundaries of E. coli as chassis for artificial photosynthesis, and due to the reported instability of ROs, we used these challenging enzymes as a model system. The light-driven approach relies on light-harvesting complexes such as eosin Y, 5(6)-carboxyeosin, and rose bengal and sacrificial electron donors (EDTA, MOPS, and MES) that were easily taken up by the cells. The obtained product formations of up to 1.3 g L?1 and rates of up to 1.6 mm h?1 demonstrate that this is a comparable approach to typical whole-cell transformations in E. coli. The applicability of this photocatalytic synthesis has been demonstrated and represents the first example of a photoinduced RO system.

Engineering P450LaMO stereospecificity and product selectivity for selective C-H oxidation of tetralin-like alkylbenzenes

The P450-mediated asymmetric hydroxylation of inert C-H bonds is a chemically challenging reaction. Self-sufficient P450LaMO from the CYP116B subfamily could catalyze the transformation of 1,2,3,4-tetrahydronaphthalene to (S)-tetralol, despite its poor enantioselectivity (er 66:34) and product selectivity (the ratio of alcohol and ketone, ak, 76:24). To improve the selectivity, phenylalanine scanning and further protein engineering were performed to reshape the active pocket of P450LaMO, resulting in a mutant (T121V/Y385F/M391L) with not only improved (S)-enantioselectivity (er 98:2) but also excellent product selectivity (ak 99:1), in contrast to another mutant L97F/T121F/E282V/T283Y with complementary (R)-enantioselectivity (er 23:77). Moreover, the enantiopure (S)-alcohols formed by the P450LaMO-catalyzed oxidation of a series of alkylbenzenes are potentially important building blocks in the pharmaceutical industry. This Phe-based enantioselectivity engineering used for reshaping the active pocket of P450s could provide a guide to the protein evolution of other CYP116B members.

Unusually Broad Substrate Profile of Self-Sufficient Cytochrome P450 Monooxygenase CYP116B4 from Labrenzia aggregata

A new member of the CYP116B subfamily - P450LaMO - was discovered in Labrenzia aggregata by genomic data mining. It was successfully overexpressed in Escherichia coli, purified, and subsequently characterized spectroscopically, and its catalytic properties were assessed. Substrate profiling of the P450LaMO revealed that it was a versatile catalyst, exhibiting hydroxylation and epoxidation activities as well as O-dealkylation and asymmetric sulfoxidation activities. Diverse compounds, including alkylbenzenes, aromatic bicyclic molecules, and terpenoids, were shown to be hydroxylated by P450LaMO. Such diverse catalytic activities are uncommon for the bacterial P450s, and the P450LaMO -mediated stereoselective hydroxylation of inactivated C - H bonds - ubiquitous and relatively unreactive in organic molecules - is particularly unusual. The self-sufficient nature of P450LaMO, coupled with its broad substrate range, highlights it as an ideal template for directed evolution towards various applications.

Unusually Broad Substrate Profile of Self-Sufficient Cytochrome P450 Monooxygenase CYP116B4 from Labrenzia aggregata

A new member of the CYP116B subfamily - P450LaMO - was discovered in Labrenzia aggregata by genomic data mining. It was successfully overexpressed in Escherichia coli, purified, and subsequently characterized spectroscopically, and its catalytic properties were assessed. Substrate profiling of the P450LaMO revealed that it was a versatile catalyst, exhibiting hydroxylation and epoxidation activities as well as O-dealkylation and asymmetric sulfoxidation activities. Diverse compounds, including alkylbenzenes, aromatic bicyclic molecules, and terpenoids, were shown to be hydroxylated by P450LaMO. Such diverse catalytic activities are uncommon for the bacterial P450s, and the P450LaMO -mediated stereoselective hydroxylation of inactivated C-H bonds - ubiquitous and relatively unreactive in organic molecules - is particularly unusual. The self-sufficient nature of P450LaMO, coupled with its broad substrate range, highlights it as an ideal template for directed evolution towards various applications.

New synthesis of A-ring aromatic strigolactone analogues and their evaluation as plant hormones in pea (pisum sativum)

A new general access to A-ring aromatic strigolactones, a new class of plant hormones, has been developed. The key transformations include in sequence ring-closing metathesis, enzymatic kinetic resolution and a radical cyclization with atom transfer to install the tricyclic ABC-ring system. The activity as plant hormones for the inhibition of shoot branching in pea of various analogues synthesized by this strategy is reported. Inhibiting shoot branching: A new general access to A-ring aromatic strigolactones (see scheme), a new class of plant hormones, has been developed. The biological activity of various analogues synthesized by this strategy for inhibiting bud outgrowth in pea was evaluated. Copyright

The effect of encapsulated Zn-POM on the catalytic activity of MIL-101 in the oxidation of alkenes with hydrogen peroxide

Zinc monosubstituted Keggin heteropolyanion [PZnMo2W 9O39]5- was electrostatically bound to nanocages of MIL-101 polymer matrix. The Zn-POM@MIL-101 catalyst was characterized by XRD, N2 adsorption, atomic absorption (AAS), and FT-IR spectroscopic methods. The catalytic activity of the new composite material, Zn-POM@MIL-101, was assessed in the oxidation of alkenes using aqueous hydrogen peroxide as oxidant. Zn-POM@MIL-101/H2O2 catalytic system demonstrated good catalytic activity in the oxidation reactions. Zn-POM@MIL-101 was reusable for three catalytic cycles. While the MIL-101 matrix is an active catalyst in these oxidation reactions, the presence of Zn-POM significantly changed the selectivity and reaction times. Copyright

Stereoselective benzylic hydroxylation of 2-substituted indanes using toluene dioxygenase as biocatalyst

Indane, 1A, and a series of 2-substituted indane substrates, 1B-1D, 1G, 1I-1L, were found to undergo benzylic monohydroxylation catalysed by toluene dioxygenase, present in the intact cells of Pseudomonas putida UV 4, to yield enantiopure cis-indan-1-ols, 2A-2D, 2G, 2I-2L of the same absolute configuration at C-1 as major bioproducts. Enantiopure trans-indan-1-ols 6B, 6C, and 6G were also obtained as minor metabolites. Evidence of further sequential benzylic hydroxylation (bis-hydroxylation) was found only with substrates 2A, 1C, 1D and 1L to yield the corresponding enantiopure trans-1,3-diols, 3A, 3C, 3D and 3L. Minor enzyme-catalysed processes also observed include benzylic alcohol oxidation to ketones (4A, 5A, 4B, 4L, 5L), ketone reduction to benzylic alcohol 6A, ester hydrolysis to indan-2-ol 1B, and cis-dihydroxylation of indan-1-ol 6A to triol 7. The enantiopurities and absolute configurations of bioproducts have been determined using MTPA ester formation, circular dichroism spectroscopy and stereochemical correlation methods. The contribution of asymmetric oxidation and kinetic resolution to the production of bioproducts of high ee (>98%), and the metabolic sequence involved in their biotransformation by P. putida UV4 is discussed. Enantiocomplementarity was found during the benzylic hydroxylation of indan-2-ol 1B, using toluene dioxygenase and naphthalene dioxygenase, when both single enantiomers of the metabolites 2B, 4B and 6B of opposite configurations were obtained.

Enantioselective Bacterial Biotransformation Routes to cis-Diol Metabolites of Monosubstituted Benzenes, Naphthalene and Benzocycloalkenes of Either Absolute Configuration

Enzyme-catalysed kinetic resolution and asymmetric dihydroxylation routes to enantiopure cis-diol metabolites of arenes and benzocycloalkenes of either absolute configuration have been developed using appropriate strains of the bacterium Pseudomonas putida.