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About This Item
Empirical Formula (Hill Notation):
C7H10O
CAS Number:
Molecular Weight:
110.15
Beilstein/REAXYS Number:
1209657
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22
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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Christiane Jung et al.
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
P J Loida et al.
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
M B Bass et al.
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
J Contzen et al.
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
Megan C Thielges et al.
The journal of physical chemistry. A, 115(34), 9714-9723 (2011-06-09)
Progress in the field of 2D IR vibrational spectroscopy has been bolstered by the production of intense mid-IR laser pulses. As higher-energy pulses are employed, a concomitant increase occurs in the likelihood of fifth-order contributions to the 2D IR spectra.
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