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Biochemical and biophysical research communications

Cyanide binding to human plasma heme-hemopexin: a comparative study.


PMID 23068104

Abstract

Hemopexin (HPX) displays a pivotal role in heme scavenging and delivery to the liver. In turn, heme-Fe-hemopexin (HPX-heme-Fe) displays heme-based spectroscopic and reactivity properties. Here, kinetics and thermodynamics of cyanide binding to ferric and ferrous hexa-coordinate human plasma HPX-heme-Fe (HHPX-heme-Fe(III) and HHPX-heme-Fe(II), respectively), and for the dithionite-mediated reduction of the HHPX-heme-Fe(III)-cyanide complex, at pH 7.4 and 20.0°C, are reported. Values of thermodynamic and kinetic parameters for cyanide binding to HHPX-heme-Fe(III) and HHPX-heme-Fe(II) are K = (4.1 ± 0.4) × 10(-6) M, k(on) = (6.9 ± 0.5) × 10(1) M(-1) s(-1), and k(off) = 2.8 × 10(-4) s(-1); and H = (6 ± 1) × 10(-1) M, h(on) = 1.2 × 10(-1) M(-1) s(-1), and h(off) = (7.1 ± 0.8) × 10(-2) s(-1), respectively. The value of the rate constant for the dithionite-mediated reduction of the HHPX-heme-Fe(III)-cyanide complex is l = 8.9 ± 0.8 M(-1/2) s(-1). HHPX-heme-Fe reactivity is modulated by proton acceptor/donor amino acid residue(s) (e.g., His236) assisting the deprotonation and protonation of the incoming and outgoing ligand, respectively.

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H9291 Hemopexin from human plasma, ≥95% (SDS-PAGE), lyophilized powder