Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase.
- 15 August 1991
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 88 (16) , 6956-6960
- https://doi.org/10.1073/pnas.88.16.6956
Abstract
Lignin peroxidase shares several structural features with the well-studied horseradish peroxidase and cytochrome c peroxidase but carries a higher redox potential. Here the heme domain of lignin peroxidase and the lignin peroxidase cyanide adduct was examined by 1HNMR spectroscopy, including nuclear Overhauser effect and two-dimensional measurements, and the findings were compared with those for horseradish peroxidase and cytochrome c peroxidase. Structural information was obtained on the orientation of the heme vinyl and propionate groups and the proximal and distal histidines. The shifts of the epsilon1 proton of the proximal histidine were found to be empirically related to the Fe3+/Fe2+ redox potentials.Keywords
This publication has 27 references indexed in Scilit:
- Magnetic resonance spectral characterization of the heme active site of Coprinus cinereus peroxidaseBiochemistry, 1989
- A nuclear Overhauser effect study of the heme crevice in the resting state and compound I of horseradish peroxidase: evidence for cation radical delocalization to the proximal histidineBiochemistry, 1988
- Enzymatic "Combustion": The Microbial Degradation of LigninAnnual Review of Microbiology, 1987
- Lignin peroxidase: resonance Raman spectral evidence for compound II and for a temperature-dependent coordination-state equilibrium in the ferric enzymeBiochemistry, 1987
- An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporiumBiochemical and Biophysical Research Communications, 1983
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Assignment of hyperfine shifted resonances in high-spin forms of cytochrome c peroxidase by reconstitutions with deuterated heminsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Axial histidyl imidazole non-exchangeable proton resonances as indicators of imidazole hydrogen bonding in ferric cyanide complexes of heme peroxidasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Assignment of exchangeable proximal histidine resonances in high-spin ferric hemoproteins: Substrate binding in horseradish peroxidaseBiochemical and Biophysical Research Communications, 1979
- Nuclear magnetic resonance studies of hemoproteins. Acid-alkaline transition, ligand binding characteristics, and structure of the heme environments in horseradish peroxidaseBiochemistry, 1977