34244-66-1

Upstream product

• 92-52-4 biphenyl 

Downstream Products

• 61664-53-7 (1S,2R,3R)-3-phenylcyclohexane-1,2-diol 
• 187837-12-3 (1S,2R)-3-phenylcyclohex-3-ene-1,2-diol 
• 57525-74-3 (1S,2R,3S)-3-phenylcyclohexane-1,2-diol 
• 580-51-8 [1,1'-biphenyl]-3-ol 
• 90-43-7 2-Phenylphenol 
• 1392229-38-7 (4R,5S)-4,5-bis((tert-butyldimethylsilyl)oxy)-3-phenylcyclohex-2-en-1-one 
• 1392229-36-5 (1S,2R-3-phenylcyclohex-3-ene-1,2-diyl)bis(oxy)bis(tert-butyldimethylsilane) 
• 1284306-63-3 (4R,5S)-4,5-dihydroxy-3-phenylcyclohex-2-enone 
• 921202-21-3 (1S,2R)-3-((3aR,7aS)-2,2-Dimethyl-3a,7a-dihydro-benzo[1,3]dioxol-4-yl)-cyclohexa-3,5-diene-1,2-diol 
• 138608-61-4 (3aR,7aS)-2,2-Dimethyl-4-phenyl-3a,7a-dihydro-benzo[1,3]dioxole 

Relevant academic research and scientific papers

Biphenyl-cis-diol chemistry to access enantiopure aryl-substituted organoiron complexes

The endo face selectivity of the complexation of the biologically derived 3-phenyl-1,2-dihydroxycyclohexa-3,5-diene ligand has been proved by an X-ray crystallographic study of the enantiopure (1R,2S,3S) η4 tricarbonyliron complex, and the correlation between the absolute configuration of the complex and its circular dichroism curve has been established to provide a basis on which to assign absolute configurations in the synthetically important ['-(Ar)CCH-CHCH-']Fe(CO)3 series.

Retuning rieske-type oxygenases to expand substrate range

Rieske-type oxygenases are promising biocatalysts for the destruction of persistent pollutants or for the synthesis of fine chemicals. In this work, we explored pathways through which Rieske-type oxygenases evolve to expand their substrate range. BphAEp4, a variant biphenyl dioxygenase generated from Burkholderia xenovorans LB400 BphAELB400 by the double substitution T335A/F336M, and BphAERR41, obtained by changing Asn338, Ile341, and Leu409 of BphAE p4 to Gln338, Val341, and Phe409, metabolize dibenzofuran two and three times faster than BphAELB400, respectively. Steady-state kinetic measurements of single- and multiple-substitution mutants of BphAELB400 showed that the single T335A and the double N338Q/L409F substitutions contribute significantly to enhanced catalytic activity toward dibenzofuran. Analysis of crystal structures showed that the T335A substitution relieves constraints on a segment lining the catalytic cavity, allowing a significant displacement in response to dibenzofuran binding. The combined N338Q/L409F substitutions alter substrate-induced conformational changes of protein groups involved in subunit assembly and in the chemical steps of the reaction. This suggests a responsive induced fit mechanism that retunes the alignment of protein atoms involved in the chemical steps of the reaction. These enzymes can thus expand their substrate range through mutations that alter the constraints or plasticity of the catalytic cavity to accommodate new substrates or that alter the induced fit mechanism required to achieve proper alignment of reactioncritical atoms or groups.

Medium-scale preparation of useful metabolites of aromatic compounds via whole-cell fermentation with recombinant organisms

The whole-cell fermentation of aromatic coumpounds with Escherichia coli JM109 (pDTG601) on a medium scale (10-15L) produces enantiopure cyclohexadienediols. A detailed procedure for the fermentation is described, and yields for several metabolites are provided. A similar procedure using E. coli JM109 (pDTG602) affords catechols. The dienediols are useful for asymmetric synthesis, and several important targets originating from these metabolites are tabulated.