Plant peroxidases crystal structure

Fig. 6. Mechanisms for the reduction of compounds I and II of HRP C by ferulic acid, after Henriksen et al. 195). This scheme is based on new information from the 1.45 A resolution crystal structure of the ternary complex of ferulic acid and cyanide-ligated HRP C 195). The direction of proton transfer is indicated by the dotted arrows. The mechanism is discussed in Section IV,B,2, and the crystal structure data in Section IV,F,4. Note that a distal site water molecule makes an important hydrogen bond with the backbone carbonyl group of Prol39 (a residue conserved in all members of the plant peroxidase superfamily).

The superfamily of plant, fungal, and bacterial heme peroxidases (also called non animal peroxidase superfamily, see Chap. 2) categorizes its components into three classes based on sequence alignment and biological origin, such as initially proposed by K.G. Welinder using the only crystal structure available at that moment (yeast CCP) as a model [3, 4]. Class III is the largest one, with over 3,000 plant peroxidase entries in PeroxiBase, followed by Classes I and II, with over 900 entries... 

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