Title : Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry.

Pub. Date : 2004 Feb 15

PMID : 14759599






4 Functional Relationships(s)
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1 Azide binding to yeast cytochrome c peroxidase and horse metmyoglobin: comparative thermodynamic investigation using isothermal titration calorimetry. Azides cytochrome-c peroxidase Saccharomyces cerevisiae S288C
2 CcP and Mb differ significantly in their reactivity toward the azide anion, N3-. Azides cytochrome-c peroxidase Saccharomyces cerevisiae S288C
3 Protonation of His-64 in Mb enhances HN3 binding due to a gating mechanism while protonation of His-52 in CcP decreases the affinity for HN3 due to loss of base-assisted association of the ligand to the heme iron. Histidine cytochrome-c peroxidase Saccharomyces cerevisiae S288C
4 Protonation of His-64 in Mb enhances HN3 binding due to a gating mechanism while protonation of His-52 in CcP decreases the affinity for HN3 due to loss of base-assisted association of the ligand to the heme iron. Iron cytochrome-c peroxidase Saccharomyces cerevisiae S288C