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Hemoglobin nitrosyl complexes

Yonetoni and co-workers (1972) have shown that hemoglobin and myoglobin form nitrosyl complexes with different bond angles at 77 K and at room temperature. The high-temperature species has less g tensor anisotropy (g = 2.03, gy = 1.98-1.99) and poorly resolved hyperfine splitting. Addition of glycerol at high concentrations prevented the transition between these forms. [Pg.90]

Sanina NA, Syrtsova LA et al (2007) Reactions of sulfiff-nitrosyl iron complexes of g=2.03 family with hemoglobin (Hb) kinetics of Hb-NO formation in aqueous solutions. Nitric Oxide 16 181-188... [Pg.108]


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See also in sourсe #XX -- [ Pg.89 , Pg.90 ]




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