Microperoxidase-11 (MP11) is an undecapeptide derived from horse heart cytochrome c (cytc). MP11 is characterized by a covalently linked solvent-exposed heme group, the heme-Fe atom being axially coordinated by a histidyl residue. Here, the reactions of ferrous and ferric MP11 (MP11-Fe(II) and MP11-Fe(III), respectively) with cyanide have been investigated from the kinetic and thermodynamic viewpoints, at pH 7.0 and 20.0 A degrees C. Values of the second-order rate constant for cyanide binding to MP11-Fe(II) and MP11-Fe(III) are 4.5 M-1 s(-1) and 8.9 x 10(3) M-1 s(-1), respectively. Values of the first-order rate constant for cyanide dissociation from ligated MP11-Fe(II) and MP11-Fe(III) are 1.8 x 10(-1) s(-1) and 1.5 x 10(-3) s(-1), respectively. Values of the dissociation equilibrium constant for cyanide binding to MP11-Fe(II) and MP11-Fe(III) are 3.7 x 10(-2) and 1.7 x 10(-7) M, respectively, matching very well with those calculated from kinetic parameters so that no intermediate species seem to be involved in the ligand-binding process. The pH-dependence of cyanide binding to MP11-Fe(III) indicates that CN- is the only binding species. Present results have been analyzed in parallel with those of several heme-proteins, suggesting that (1) the ligand accessibility to the metal center and cyanide ionization may modulate the formation of heme-Fe-cyanide complexes, and (2) the general polarity of the heme pocket and/or hydrogen bonding of the heme-bound ligand may affect cyanide exit from the protein matrix.
Ascenzi, P., Sbardella, D., Santucci, R., & Coletta, M. (2016). Cyanide binding to ferrous and ferric microperoxidase-11. JBIC, 21(4), 511-522.
|Titolo:||Cyanide binding to ferrous and ferric microperoxidase-11|
|Data di pubblicazione:||2016|
|Citazione:||Ascenzi, P., Sbardella, D., Santucci, R., & Coletta, M. (2016). Cyanide binding to ferrous and ferric microperoxidase-11. JBIC, 21(4), 511-522.|
|Appare nelle tipologie:||1.1 Articolo in rivista|