23357-45-1Relevant articles and documents
Benzocycloarene hydroxylation by P450 biocatalysis
Mayhew, Martin P.,Roitberg, Adrian E.,Tewari, Yadu,Holden, Marcia J.,Vanderah, David J.,Vilker, Vincent L.
, p. 35 - 42 (2002)
Experimental and theoretical studies of the hydroxylation of a family of benzocycloarene compounds [benzocyclobutene, benzocyclopentene (indan), benzocyclohexene (tetralin), and benzocycloheptene] by wild type and Y96F mutant P450cam were performed in order to understand the factors affecting product distribution, catalytic rate and cofactor utilization. The products of all reactions except that of benzocycloheptene were regiospecifically hydroxylated in the 1-position. Reaction energetics predominated over active site steric constraints in this case so that quantum mechanical calculations (B3LYP/6-31G*) comparing the energetics of all possible radical intermediates successfully predicted hydroxylation at the 1- and 3-positions of benzocycloheptene, and at the 1-position for the other three compounds. However, the fact that the ratio of 1-alcohol to 3-alcohol changes significantly between wild type and Y96F mutant P450cam indicates that active site geometry and composition also play a significant role in determining BCA7 product regiospecificity. The indan and tetralin reaction products were stereoselective for the R enantiomer (88 and 94%, respectively). Steric constraints of the active site were confirmed by molecular dynamics calculations (locally enhanced sampling dynamics) to control enantiomer distribution for tetralin hydroxylation. NADH coupling, binding affinity, and product turnover rates were dramatically higher for Y96F P450cam, showing that the removal of the active site hydroxyl group on tyrosine makes the enzyme better suited for oxidation of these hydrophobic compounds. NADH coupling, binding affinity and product turnover rate for each enzyme generally increased with arene ring size. For both enzymes, NADH coupling and product turnover rates were correlated with the extent of high-spin shift upon substrate binding as determined by the shift in Soret absorption bands at 417 and 391 nm.
Enantioselective benzylic hydroxylation of indan and tetralin with Pseudomonas monteilii TA-5
Lie, Felicia,Chen, Yongzheng,Wang, Zunsheng,Li, Zhi
, p. 1206 - 1211 (2009)
A set of 22 toluene- and ethylbenzene-degrading strains were screened for the enantioselective benzylic hydroxylation of indan and tetralin, and Pseudomonas monteilii TA-5 was discovered as an active and selective biocatalyst for such hydroxylations. Cells of P. monteilii TA-5 can be easily grown to a high density and demonstrated a specific hydroxylation activity of 24 U/g cdw (cell dry weight). Conditions for the hydroxylation of indan 1a and tetralin 1b with resting cells of this strain were optimized, to give the corresponding (R)-1-indanol 2a and (R)-1-tetralol 2b in 99% ee and 62-67% yields, respectively. No significant product inhibition was observed, and biohydroxylation with cell-free extracts suggested that the responsible hydroxylase is a soluble enzyme depending on either NADH or NADPH. Preparative biohydroxylation was demonstrated with resting cells as biocatalysts, affording (R)-2a in 99% ee and 65% yield, and (R)-2b in 99% ee and in 63% yield, respectively.
Concurrent oxidations with tandem biocatalysts in one pot: Green, selective and clean oxidations of methylene groups to ketones
Zhang, Wei,Tang, Weng Lin,Wang, Daniel I. C.,Li, Zhi
, p. 3284 - 3286 (2011)
A novel tandem-biocatalysts system consisting of a monooxygenase-containing microorganism and an alcohol dehydrogenase is developed for the concurrent oxidations of methylene groups to ketones in one pot, providing green, clean and simple access to valuable ketones with high yield, excellent selectivity and efficient cofactor recycling.
Designer Outer Membrane Protein Facilitates Uptake of Decoy Molecules into a Cytochrome P450BM3-Based Whole-Cell Biocatalyst
Karasawa, Masayuki,Shoji, Osami,Stanfield, Joshua Kyle,Suzuki, Kazuto,Yonemura, Kai
supporting information, (2021/12/16)
We report an OmpF loop deletion mutant, which improves the cellular uptake of external additives into an Escherichia coli whole-cell biocatalyst. Through co-expression of the OmpF mutant with wild-type P450BM3 in the presence of decoy molecules, the yield
Chiral Yolk-Shell MOF as an Efficient Nanoreactor for Asymmetric Catalysis in Organic-Aqueous Two-Phase System
Shi, Shunli,Zhong, Yicheng,Hu, Zhuo,Wang, Lei,Yuan, Mingwei,Ding, Shunmin,Wang, Shuhua,Chen, Chao
supporting information, p. 12714 - 12718 (2021/09/11)
It remains a great challenge to introduce large and efficient homogeneous asymmetric catalysts into MOFs and other microporous materials as well as retain their degrees of freedom. Herein, a new heterogeneous strategy of homogeneous chiral catalysts is proposed, that is, to construct a yolk-shell MOFs-confined, large-size, and highly efficient homogeneous chiral catalyst, which can be used as a nanoreactor for asymmetric catalytic reactions.
Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst
Gavin, Declan P.,Murphy, Edel J.,Foley, Aoife M.,Castilla, Ignacio Abreu,Reen, F. Jerry,Woods, David F.,Collins, Stuart G.,O'Gara, Fergal,Maguire, Anita R.
, p. 2466 - 2474 (2019/03/11)
Evaluation of an esterase annotated as 26D isolated from a marine metagenomic library is described. Esterase 26D was found to have a unique substrate scope, including synthetic transformations which could not be readily effected in a synthetically useful manner using commercially available enzymes. Esterase 26D was more selective towards substrates which had larger, more sterically demanding substituents (i. e. iso-propyl or tert-butyl groups) on the β-carbon, which is in contrast to previously tested commercially available enzymes which displayed a preference for substrates with sterically less demanding substituents (e.g. methyl group) at the β-carbon. (Figure presented.).
