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. 2018 Nov 1;29(18):1841–1857. doi: 10.1089/ars.2017.7368

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Copyright 2018, Mary Ann Liebert, Inc., publishers

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FIG. 6. — Spectral characterization of HO2 in the Fe³⁺-heme-bound forms. (A) Absorbance spectra of 5 μM Fe³⁺-heme-bound forms of HO2_core (^…), HO2_tail^R (), and HO2_sol^R (—) in 50 mM Tris (pH 8.0) and 50 mM KCl at 20°C. (B) EPR spectra of the Fe³⁺-heme-bound forms of HO2_core, HO2_sol^R, HO2_tail^R, and the His45Ala variant of HO2_sol^R. The g values are indicated above the spectra. (C) Absorbance spectra of 5 μM Fe³⁺-heme-bound forms of HO2_tail^R (—), HO2_tail(C282A)^R (), and HO2_tail(C265A)^R (^…) in 50 mM Tris (pH 8.0) and 50 mM KCl at 20°C. (D) A model of heme binding to the oxidized form of HO2_sol, which has a single heme-binding site due to the participation of Cys265 and Cys282 in a disulfide bond, and the reduced form of HO2_sol, which has three heme-binding sites. Below each heme-binding site are the characteristics of that site, including the maximum absorbance, the g-values, the K_d values obtained by equilibrium titrations [K_d (equil)], and the k_off/k_on values obtained by kinetic measurements. The figures in (A–C) are reprinted (adapted) with permission from Fleischhacker et al. (20). Copyright (2015) American Chemical Society. EPR, electron paramagnetic resonance; HO2_core, HO2 spanning residues 1-248; HO2^R, HO2 in the disulfide bond-reduced form; HO2_sol, HO2 spanning residues 1-288; HO2_tail, HO2 spanning residues 213-288. EPR, electron paramagnetic resonance; HO2_core, HO2 spanning residues 1-248; HO2^R, HO2 in the disulfide bond-reduced form; HO2_sol, HO2 spanning residues 1-288; HO2_tail, HO2 spanning residues 213-288.

Inline graphic — Spectral characterization of HO2 in the Fe³⁺-heme-bound forms. (A) Absorbance spectra of 5 μM Fe³⁺-heme-bound forms of HO2_core (^…), HO2_tail^R (), and HO2_sol^R (—) in 50 mM Tris (pH 8.0) and 50 mM KCl at 20°C. (B) EPR spectra of the Fe³⁺-heme-bound forms of HO2_core, HO2_sol^R, HO2_tail^R, and the His45Ala variant of HO2_sol^R. The g values are indicated above the spectra. (C) Absorbance spectra of 5 μM Fe³⁺-heme-bound forms of HO2_tail^R (—), HO2_tail(C282A)^R (), and HO2_tail(C265A)^R (^…) in 50 mM Tris (pH 8.0) and 50 mM KCl at 20°C. (D) A model of heme binding to the oxidized form of HO2_sol, which has a single heme-binding site due to the participation of Cys265 and Cys282 in a disulfide bond, and the reduced form of HO2_sol, which has three heme-binding sites. Below each heme-binding site are the characteristics of that site, including the maximum absorbance, the g-values, the K_d values obtained by equilibrium titrations [K_d (equil)], and the k_off/k_on values obtained by kinetic measurements. The figures in (A–C) are reprinted (adapted) with permission from Fleischhacker et al. (20). Copyright (2015) American Chemical Society. EPR, electron paramagnetic resonance; HO2_core, HO2 spanning residues 1-248; HO2^R, HO2 in the disulfide bond-reduced form; HO2_sol, HO2 spanning residues 1-288; HO2_tail, HO2 spanning residues 213-288. EPR, electron paramagnetic resonance; HO2_core, HO2 spanning residues 1-248; HO2^R, HO2 in the disulfide bond-reduced form; HO2_sol, HO2 spanning residues 1-288; HO2_tail, HO2 spanning residues 213-288.