Fig. 5: The active site in AmVHPO is formed by two adjacent subunits. | Nature Communications

Fig. 5: The active site in AmVHPO is formed by two adjacent subunits.

From: Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases

Fig. 5

a Coil representation of neighboring subunits in the AmVHPO:TMB-R425S complex. The phosphate mimicking the catalytic vanadate is coordinated by one subunit, while the substrate binding channel is formed together with the adjacent subunit. The loop region from the flanking subunit is crucial for TMB binding (loop region, residues 390–404, highlighted in cyan) and is structured only in the R425S mutant. b Close-up view of the active site with protein side chains engaged in ligand and phosphate binding. S425 is colored pink. c Proposed schematic mechanism of enzymatic chlorination in R425S-AmVHPO. d Preliminary substrate scope of the R425S-catalyzed chlorination in comparison with those addressable by wild-type AmVHPO and NCS/DABCO. aisolated yield using R425S-AmVHPO as catalyst; byields determined by LC-MS or GC-MS using wild-type AmVHPO as catalyst; cisolated yield using NCS/DABCO; n.r. no reaction; r.r. ratio of regioisomers. TMB = 1,3,5-trimethoxybenzene; NCS/DABCO = N-hydroxysuccinimide/1,4-Diazabicyclo[2.2.2]octan.

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