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About 3 tyrosine residues of cytochrome P-450 LM2 are accessible to chemical modification with tetranitromethane. Nitration of two tyrosines inactivates the enzyme to about 20%. The partial formation of a hyper-porphyrin spectrum originating from the pK shift by nitration and formation of a tyrosinate is prevented by modification in the presence of the inhibitor metyrapone. These findings support...
The relaxation kinetics of the temperature-dependent spin equilibrium of cytochrome P450 LM2 has been resolved by means of a laser temperature-jump device. The Nd laser system in the Q-switched mode delivers 3 J/25 ns pulses which were Raman shifted to 1.89 μm by use of a high pressure H 2 -gas cell. The LM2 equilibrium relaxation proceeds in the ns-range, the rate constants of the on- and...
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