TY  - GEN
AB  - 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.
AD  - Oregon Health and Science University
AU  - Youngs, Heather
DA  - 2003-05-01
DO  - 10.6083/M40Z71K5
DO  - DOI
ED  - Gold, Michael
ED  - Loehr, Thomas
ED  - Advisor
ED  - Advisor
ID  - 2413
KW  - Mutagenesis, Site-Directed
KW  - Polymers
KW  - Lignin
L1  - https://digitalcollections.ohsu.edu/record/2413/files/3150_etd.pdf
L2  - https://digitalcollections.ohsu.edu/record/2413/files/3150_etd.pdf
L4  - https://digitalcollections.ohsu.edu/record/2413/files/3150_etd.pdf
LK  - https://digitalcollections.ohsu.edu/record/2413/files/3150_etd.pdf
N2  - 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.
PB  - Oregon Health and Sciences University
PY  - 2003-05-01
T1  - Structure/function studies  of  manganese peroxidase
TI  - Structure/function studies  of  manganese peroxidase
UR  - https://digitalcollections.ohsu.edu/record/2413/files/3150_etd.pdf
Y1  - 2003-05-01
ER  -