The closeness of the phenol ring rotation angle θ in the six tyrosines in Hb to the target value of either 53.65° (average of the 53° and 54.3° angles reported in Fig. 6) or its complementary angle of 66.35° (see Materials and methods).

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The closeness of the phenol ring rotation angle θ in the six tyrosines in Hb to the target value of either 53.65° (average of the 53° and 54.3° angles reported in Fig. 6 ) or its complementary angle of 66.35° (see Materials and methods).

2020, 34(4): 281-291.

Tyrosyl radical in haemoglobin and haptoglobin-haemoglobin complex: how does haptoglobin make haemoglobin less toxic? .

Figures of the Article

Consecutively measured spectra of 340 μmol/L metHb (by haem) reacting with 1360 mmol/L H₂O₂ (a 4-fold excess of peroxide over haem).
Magnetic field range of a spectrum as reported by the Teslameter at different spectra scan rates.
Kinetic dependences of the tyrosyl free radical in the mixtures of 340 μmol/L human metHb and 1.36 mmol/L H₂O₂ (both concentrations are final), at different pH values.
Liquid phase EPR spectra of Tyr radical in Hb and Hp-Hb.
Kinetic dependences of the tyrosyl radical in the Hb+H₂O₂ and Hp-Hb+H₂O₂ systems.
The averaged EPR spectra of the free radicals formed under H₂O₂ addition to Hb and to the Hp-Hb complex (the same as shown in Fig. 4 ) and their simulations as tyrosyl radical EPR signals.
A ρ-g chart^[18,33] showing the principal g-factor sets for the tyrosyl radicals in Hb and Hp-Hb.
The closeness of the phenol ring rotation angle θ in the six tyrosines in Hb to the target value of either 53.65° (average of the 53° and 54.3° angles reported in Fig. 6 ) or its complementary angle of 66.35° (see Materials and methods).

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