@article{ETD,
      recid = {2413},
      author = {Youngs, Heather},
      title = {Structure/function studies  of  manganese peroxidase},
      publisher = {Oregon Health and Sciences University},
      school = {Ph.D.},
      address = {2003-05-01},
      number = {ETD},
      abstract = {Lignin is a cell wall polymer that provides rigidity, cell  adhesion, andmicrobial  resistance  to  vascular  plants. A   sort  of  natural  plastic,  lignin contains  more than   13 different  randomly  arranged chemical  linkages  and   is  responsible  for sequestering  roughly  25 %  of  the   world's  terrestrial biomass. The resulting heterogeneous   three-dimensional  matrix  is  resistant  to  enzymatic  hydrolysis  and  is chemically  stable under  most   environmental  conditions. White-rot  fungi are the  only  organisms capable of  completely  degrading  the  lignin  polymer,  and  manganese peroxidase  is  a key  enzyme in   this  process. It  is  the  only  enzyme known  that  selectively  binds  Mn2+, oxidizes  it  and  releases   Mn3+. In this  work,  the unique  Mn- binding  site  of   the  enzyme was  probed  by  site-directed  mutagenesis.},
      url = {http://digitalcollections.ohsu.edu/record/2413},
      doi = {https://doi.org/10.6083/M40Z71K5},
}