The role of Glu39 in MnII binding and oxidation by manganese peroxidase from Phanerochaete chrysoporium

Biochemistry
Heather L YoungsM H Gold

Abstract

Manganese peroxidase (MnP) is a heme-containing enzyme produced by white-rot fungi and is part of the extracellular lignin degrading system in these organisms. MnP is unique among Mn binding enzymes in its ability to bind and oxidize Mn(II) and efficiently release Mn(III). Initial site-directed mutagenesis studies identified the residues E35, E39, and D179 as the Mn binding ligands. However, an E39D variant was recently reported to display wild-type Mn binding and rate of oxidation, calling into question the role of E39 as an Mn ligand. To investigate this hypothesis, we performed computer modeling studies which indicated metal-ligand bond distances in the E39D variant and in an E35D--E39D--D179E triple variant which might allow Mn binding and oxidation. To test the model, we reconstructed the E35D and E39D variants used in the previous study, as well as an E39A single variant and the E35D--E39D--D179E triple variant of MnP isozyme 1 from Phanerochaete chrysosporium. We find that all of the variant proteins are impaired for Mn(II) binding (K(m) increases 20--30-fold) and Mn(II) oxidation (k(cat) decreases 50--400-fold) in both the steady state and the transient state. In particular, mutation of the E39 residue in MnP decreases ...Continue Reading

Citations

Nov 7, 2008·Journal of Experimental Botany·Francisco J Ruiz-DueñasAngel T Martínez
Mar 11, 2008·Applied and Environmental Microbiology·Takahisa TsukiharaTakashi Watanabe
Jan 12, 2013·ACS Chemical Biology·Rahul SinghLindsay D Eltis
Oct 6, 2006·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Thomas D PfisterYi Lu
Sep 15, 2006·Fungal Genetics and Biology : FG & B·Phil Kersten, Dan Cullen
Jul 30, 2008·FEMS Microbiology Reviews·Ri-He PengQuan-Hong Yao
Jun 3, 2021·International Journal of Molecular Sciences·Yasushi Sugano, Toru Yoshida

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