Manganese peroxidase crystal structures

Crystal structures of manganese catalases (in the (111)2 oxidation state) from Lactobacillus plantarum,its azide-inhibited complex, " and from Thermus thermophilus have been determined. There are differences between the structures that may reflect distinct biological functions for the two enzymes, the L. plantarum enzyme functions only as a catalase, while the T. thermo-philus enzyme may function as a catalase/peroxidase. The active sites are conserved in the two enzymes and are shown schematically in Figure 32. Each subunit contains an Mu2 active site,... 

Fig. 3.2 Solvent access surface (colors represent electrostatic potentials) showing the main channel providing access to the heme cofactor (in yellow bars) occupying a central cavity (heme pocket) and the second narrow channel present in some peroxidases, such as manganese-oxidizing peroxidases, accessing to the heme propionates (based on the crystal structure of P. eryngii VP, PDB 2BOQ)...

Sundaramoorthy M, Youngs HL, Gold MH et al (2005) High-resolution crystal structure of manganese peroxidase substrate and inhibitor complexes. Biochemistry 44 6463-6470... 

Sundaramoorthy M, Kishi K, Gold MH et al (1997) Crystal structures of substrate binding site mutants of manganese peroxidase. J Biol Chem 272 17574—17580... 

M Sundaramoorthy, K Kishi, MH Gold, TL Poulos. The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution. J Biol Chem 269(52) 32759-32767, 1994. 

Manganese peroxidase (MnP) is an unique enzyme in many respects. It is an extracellular enzyme that involves a heme protoporphyrin IX for the oxidation of Mn" to Mn " 94, 95). A crystal structure at 2.06-A resolution of the manganese peroxidase from the white rot basidiomycete Phanerocaete chrysosporium, which utilizes this enzyme to degrade lignin, appeared in 1994 96). The active site (Fig. 5) and the overall structure are quite similar to lignin peroxidase (LiP),... 

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