N32601
Norcamphor
98%
Synonym(s):
2-Norbornanone, Bicyclo[2.2.1]heptan-2-one
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About This Item
Recommended Products
Quality Level
Assay
98%
form
crystals
bp
168-172 °C (lit.)
mp
93-96 °C (lit.)
SMILES string
O=C1C[C@@H]2CC[C@H]1C2
InChI
1S/C7H10O/c8-7-4-5-1-2-6(7)3-5/h5-6H,1-4H2/t5-,6+/m1/s1
InChI key
KPMKEVXVVHNIEY-RITPCOANSA-N
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Related Categories
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Sol. 1
Storage Class Code
4.1B - Flammable solid hazardous materials
WGK
WGK 3
Flash Point(F)
91.4 °F - closed cup
Flash Point(C)
33 °C - closed cup
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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The Journal of biological chemistry, 263(7), 3164-3170 (1988-03-05)
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 indicate that each molecule is hydroxylated with quite different regio-specificity when metabolized
European journal of biochemistry, 269(12), 2989-2996 (2002-06-20)
The high-pressure stopped-flow technique is applied to study the CO binding in cytochrome P450cam (P450cam) bound with homologous substrates (1R-camphor, camphane, norcamphor and norbornane) and in the substrate-free protein. The activation volume DeltaV # of the CO on-rate is positive
Biochemistry, 37(13), 4317-4324 (1998-04-29)
Step-scan time-resolved Fourier transform infrared spectroscopy with a time resolution of 5 micros was applied to the carbon monoxide complex of cytochrome P-450cam (CYP101) to study the bimolecular ligand-rebinding process after flash photolysis. Spectral changes in the CO ligand stretch
Proteins, 13(1), 26-37 (1992-05-01)
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. Chem. Soc. 109:3754-3760, 1987). The present study
The Journal of biological chemistry, 270(10), 5326-5330 (1995-03-10)
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 P450cam with respect to the product profile, steady state
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