Results: 4

1.
Figure 2

Figure 2. From: Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450.

The low frequency rR spectra of ferric CYP2B4, wild-type BHT-bound (A) and F429H mutant BHT-bound (B). Spectra measured with 356 nm excitation line and normalized to the ν7 mode at 676 cm−1.

Piotr J. Mak, et al. Angew Chem Int Ed Engl. ;51(41):10403-10407.
2.
Figure 1

Figure 1. From: Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450.

The low (left) and high (right) frequency rR spectra of ferric CYP2B4, wild-type substrate-free (A), wild-type BHT-bound (B), F429H mutant substrate-free (C) and F429H mutant BHT-bound. Spectra measured with 406 nm excitation line and normalized to the ν3 mode.

Piotr J. Mak, et al. Angew Chem Int Ed Engl. ;51(41):10403-10407.
3.
Figure 4

Figure 4. From: Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450.

The high frequency rR spectra of ferrous CO adducts of substrate-free wild-type CYP2B4 (A) and F429H mutant (B). Spectra were normalized to the glycerol mode at 1468 cm−1. The traces (C) and (D) are difference traces of ferrous CO adducts of CYP2B4 wild-type and 429H mutant in substrate-free form (C) and in BHT-bound state (D).

Piotr J. Mak, et al. Angew Chem Int Ed Engl. ;51(41):10403-10407.
4.
Figure 3

Figure 3. From: Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450.

The low (left) and high (right) frequency rR spectra of ferrous CO adducts of CYP2B4, wild-type substrate-free (A), wild-type BHT-bound (B), F429H mutant substrate-free (C) and F429H mutant BHT-bound (D). Spectra measured with 442 nm excitation line and normalized to the ν7 and ν4 modes for low and high frequency region, respectively. The bottom graph shows linear correlation between ν(Fe-C) and ν(C-O) frequencies, the open squares represent wild type truncated CYP2B4,[40] the solid squares indicate points for F429H mutants and the stars show mammalian NOSs.[37–39]

Piotr J. Mak, et al. Angew Chem Int Ed Engl. ;51(41):10403-10407.

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