[New therapeutically active basic ethers. 3. 2-Aryl-, especially aralkyl-norborneol derivatives].

K STACH; W WINTER

Home/Archive/PubMed

PubMed · 13916038

[New therapeutically active basic ethers. 3. 2-Aryl-, especially aralkyl-norborneol derivatives].

K STACH·W WINTER

View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Camphor Ethers CAMPHOR/related compounds ETHERS/pharmacology Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

K STACH, W WINTER. 1962. [New therapeutically active basic ethers. 3. 2-Aryl-, especially aralkyl-norborneol derivatives].. https://pubmed.ncbi.nlm.nih.gov/13916038/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2006

Novel configurational structures of sodium tetrakis(3-heptafluorobutylryl-(+)-camphorato) Ln(III) complexes with a trapped Na+ by Na+...FC interactions in the solid state and in solution.

For newly prepared sodium tetrakis(3-heptafluorobutylryl-(+)-camphorato) Ln(III) complexes, the X-ray crystal analysis revealed an unprecedented pseudo-achiral dodecahedron (DD-8 (D(2d))), whereas in CHCl3 solution, the exciton CD and 19F NMR spectra showed a novel chiral Delta-SAPR-8 (C4) configuration which is stereospecifically formed by a trapped Na+ ion with Na+...FC (fluorocarbon) interactions.

Camphor↗

PubMed2006

Increasing the catalytic performance of a whole cell biocatalyst harboring a cytochrome p450cam system by stabilization of an electron transfer component.

Catalytic activity of a recombinant Escherichia coli whole cell biocatalyst harboring a cytochrome P450cam monooxygenase system from Pseudomonas putida coupled with enzymatic co-factor regeneration was investigated. About 0.7 micromol camphor was hydroxylated per mg dry cells at 4 degrees C in 50 mM Tris/HCl buffer (pH 7.4) when utilizing a stable putidaredoxin (Pdx) mutant, C73S/C85S-Pdx (Cys73Ser, Cys85Ser double mutant), instead of wild-type Pdx, which was about two-fold improvement in the substrate conversion. Ten-micromole camphor was completely hydroxylated at 20 degrees C in 6 h by 15 mg dry cell weight of whole cell biocatalyst including C73S/C85S-Pdx. Thus, modulation of protein-protein interaction in multicomponent enzymatic catalysis in whole cells is important.

Camphor↗

PubMed2006

The effect of heme environment on the hydrogen abstraction reaction of camphor in P450cam catalysis: a QM/MM study.

The discrepancies between the published QM/MM studies (Schöneboom, J. C.; Cohen, S.; Lin, H.; Shaik, S.; Thiel, W. J. Am. Chem. Soc. 2004, 126, 4017; Guallar, V.; Friesner, R. A. J. Am. Chem. Soc. 2004, 126, 8501) on H-abstraction of camphor in P450cam have largely been resolved. The crystallographic water molecule 903 situated near the oxo atom of Compound I acts as a catalyst for H-abstraction, lowering the barrier by about 4 kcal/mol. Spin density at the A-propionate side chain of heme can occur in the case of incomplete screening but has no major effect on the computed barrier.

Camphor↗