skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
; ;  [1];  [2];  [3]
  1. Univ. of Florence (Italy)
  2. Pennsylvania State Univ., University Park, PA (United States)
  3. 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