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- Title
Kinetics of cyanide and carbon monoxide dissociation from ferrous human haptoglobin:hemoglobin(II) complexes.
- Authors
Ascenzi, Paolo; De Simone, Giovanna; Tundo, Grazia R.; Coletta, Massimo
- Abstract
Haptoglobin (Hp) counterbalances the adverse effects of extra-erythrocytic hemoglobin (Hb) trapping the αβ dimers of Hb. In turn, the Hp:Hb complexes display heme-based reactivity. Here, the kinetics of cyanide and carbon monoxide dissociation from ferrous-ligated Hp:Hb complexes are reported at pH 7.0 and 20.0 °C. Cyanide dissociation from Hp1-1:Hb(II)-CN− and Hp2-2:Hb-CN− has been followed upon the dithionite-mediated conversion of ferric to ferrous-ligated Hp:Hb complexes. Values of kon for the dithionite-mediated reduction of Hp1-1:Hb(III)-CN− and Hp2-2:Hb(III)-CN− are (7.3 ± 1.1) × 106 M−1 s−1 and (6.2 ± 1.0) × 106 M−1 s−1, respectively. Values of the first-order rate constant (i.e., h) for cyanide dissociation from Hp1-1:Hb(II)-CN− and Hp2-2:Hb(II)-CN− are (1.2 ± 0.2) × 10−1 s−1 and (1.3 ± 0.2) × 10−1 s−1, respectively. CO dissociation from Hp:Hb(II)-CO complexes has been followed by replacing CO with NO. Values of the first-order rate constant (i.e., l) for CO dissociation from Hp1-1:Hb(II)-CO are (1.4 ± 0.2) × 10−2 s−1 and (6.2 ± 0.8) × 10−3 s−1, and those from Hp2-2:Hb(II)-CO are (1.3 ± 0.2) × 10−2 s−1 and (7.3 ± 0.9) × 10−3 s−1. Values of kon, h, and l correspond to those reported for the R-state of tetrameric Hb and isolated α and β chains. This highlights the view that the conformation of the Hb αβ-dimers bound to Hp1-1 and Hp2-2 matches that of the R-state of the Hb tetramer. Furthermore, unlike ferric Hb(III), ligated ferrous Hb(II) does not show an assembly-linked structural change.
- Subjects
HAPTOGLOBINS; CARBON monoxide; CYANIDES; ANALYTICAL mechanics
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2020, Vol 25, Issue 3, p351
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-020-01766-3