NORCAMPHOR
NORCAMPHOR structure
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Common Name | NORCAMPHOR | ||
|---|---|---|---|---|
| CAS Number | 497-38-1 | Molecular Weight | 110.154 | |
| Density | 1.1±0.1 g/cm3 | Boiling Point | 170.0±0.0 °C at 760 mmHg | |
| Molecular Formula | C7H10O | Melting Point | 93-96 °C(lit.) | |
| MSDS | Chinese USA | Flash Point | 33.9±0.0 °C | |
| Symbol |
GHS02 |
Signal Word | Danger | |
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Conformational landscape and the selectivity of cytochrome P450cam.
J. Phys. Chem. B 119 , 6620-7, (2015) Conformational heterogeneity and dynamics likely contribute to the remarkable activity of enzymes but are challenging to characterize experimentally. These features are of particular interest within the cytochrome P450 class of monooxygenases, which are of gr... |
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Role of protein and substrate dynamics in catalysis by Pseudomonas putida cytochrome P450cam.
Biochemistry 41(49) , 14499-508, (2002) The role of protein structural flexibility and substrate dynamics in catalysis by cytochrome P450 enzymes is an area of current interest. We have addressed these in cytochrome P450(cam) (P450(cam)) and its Y96A mutant with camphor and its related compounds us... |
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Conformational relaxation in hemoproteins: the cytochrome P-450cam case.
Biochemistry 39(46) , 14219-31, (2000) Photodissociation of (CO)P-450(cam)(substrate) complexes was found to trigger a conformational relaxation process that interferes with ligand rebinding at temperatures as low as 140 K even though the protein conformational substates (CS(1)) remain frozen. To ... |
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Regiodivergent Baeyer-Villiger oxidation of fused ketones by recombinant whole-cell biocatalysts.
ChemSusChem 1(1-2) , 143-8, (2008) Recombinant Escherichia coli cells expressing monooxygenases of different bacterial origin were evaluated in microbial Baeyer-Villiger oxidations of racemic fused ketones. During the enzymatic oxidation process, both the "normal" lactone generated by migratio... |
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The effect of proton donors on the facial stereoselectivity in SmI2 reduction of norcamphor.
J. Org. Chem. 76(5) , 1355-60, (2011) The endo/exo product ratio in the reactions of SmI(2) with norcamphor in the presence of various proton donors was determined. The effect of MeOH, EtOH, trifluoroethanol (TFE), ethylene glycol (EG), and water was investigated at various concentrations of thes... |
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Calculation of electronic circular dichroism spectra with time-dependent double-hybrid density functional theory.
J. Phys. Chem. A 113(4) , 767-76, (2009) Time-dependent double-hybrid density functional theory is applied to the calculation of the electronic circular dichroism (CD) spectra of molecules. The TD-B2PLYP method is based on vertical excitation energies obtained from its hybrid-GGA part B2LYP in a con... |
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Substrate mobility in a deeply buried active site: analysis of norcamphor bound to cytochrome P-450cam as determined by a 201-psec molecular dynamics simulation.
Proteins 13(1) , 26-37, (1992) While cytochrome P-450cam catalyzes the hydroxylation of camphor to 5-exo-hydroxycamphor with 100% stereospecificity, norcamphor is hydroxylated by this enzyme yielding 45% 5-exo-, 47% 6-exo-, and 8% 3-exo-hydroxynorcamphor (Atkins, W.M., Sligar, S.G., J. Am.... |
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The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
Biochemistry 28(2) , 917-22, (1989) The crystal structures of cytochrome P-450CAM complexed with the alternative substrates norcamphor and adamantanone have been refined at 2.0-A resolution and compared with the native, camphor-bound form of the enzyme. Norcamphor lacks the 8-, 9-, and 10-methy... |
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Theoretical study of the product specificity in the hydroxylation of camphor, norcamphor, 5,5-difluorocamphor, and pericyclocamphanone by cytochrome P-450cam.
J. Biol. Chem. 263(7) , 3164-70, (1988) The hydroxylations of d-camphor, norcamphor, pericyclocamphanone, and 5,5-difluorocamphor by cytochrome P-450cam have been examined using theoretical methods to identify and characterize properties which determine product specificity. Experimental results ind... |
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Stereoselective hydroxylation of norcamphor by cytochrome P450cam. Experimental verification of molecular dynamics simulations.
J. Biol. Chem. 270(10) , 5326-30, (1995) The stereoselectivity of cytochrome P450cam hydroxylation has been investigated with the enantiomerically pure substrate analog norcamphor. (1R)- and (1S)-norcamphor (> 92 enantiomeric excess) were characterized in the hydroxylation reaction with cytochrome P... |