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Poulos-Kraut mechanism

Derat E, Shaik S (2006) The Poulos-Kraut mechanism of Compound I formation in horseradish peroxidase a QM/MM study. J Phys Chem B 110 10526—10533... [Pg.103]

Fig. 5.4 Schematic representation of the Poulos-Kraut peroxidase mechanism in which the conserved distal histidine serves as an acid-base catalyst that transfers a proton from the H202 to the terminal oxygen after formation of the [Fe(III)-OOH] intermediate. The proximal histidine iron ligand and the catalytic histidine and arginine are shown. In HRP, these residues are His 170,... Fig. 5.4 Schematic representation of the Poulos-Kraut peroxidase mechanism in which the conserved distal histidine serves as an acid-base catalyst that transfers a proton from the H202 to the terminal oxygen after formation of the [Fe(III)-OOH] intermediate. The proximal histidine iron ligand and the catalytic histidine and arginine are shown. In HRP, these residues are His 170,...
See other pages where Poulos-Kraut mechanism is mentioned: [Pg.83]    [Pg.351]    [Pg.83]    [Pg.351]    [Pg.138]    [Pg.21]    [Pg.97]    [Pg.125]    [Pg.126]   
See also in sourсe #XX -- [ Pg.83 ]

See also in sourсe #XX -- [ Pg.351 ]



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