Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase
- Univ. of Florence (Italy)
- Pennsylvania State Univ., University Park, PA (United States)
- Dept. of Agriculture, Madison, WI (United States)
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 {sup 1}H NMR 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 {var epsilon}1 proton of the proximal histidine were found to be empirically related to the Fe{sup 3+}/Fe{sup 2+} redox potentials.
- DOE Contract Number:
- FG02-87ER13690
- OSTI ID:
- 5701127
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:16; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
LIGNIN
BIODEGRADATION
PEROXIDASES
NUCLEAR MAGNETIC RESONANCE
CHEMICAL SHIFT
CYTOCHROME OXIDASE
HISTIDINE
PHANEROCHAETE
PROTONS
REDOX POTENTIAL
AMINO ACIDS
AZOLES
BARYONS
CARBOHYDRATES
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
DECOMPOSITION
ELEMENTARY PARTICLES
ENZYMES
EUMYCOTA
FERMIONS
FUNGI
HADRONS
HAEM DEHYDROGENASES
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
IMIDAZOLES
MAGNETIC RESONANCE
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDOREDUCTASES
PLANTS
POLYSACCHARIDES
PROTEINS
RESONANCE
SACCHARIDES
550600* - Medicine