Monoclinic crystals of lignin peroxidase

Lignin Peroxidase Of

Ligninase is a generic name for a group of isozymes that catalyze the oxidative depolymerization of lignin. Although undoubtedly produced by other lignin-degrading fungi, these isozymes to data have been isolated only from the basidiomycete Phanerochaete chrysosporium Burds. 1,2 These ligninases are extracellular and are produced during secondary metabolism, brought about by nutrient starvation...

Lignin Peroxidase Compound III

Lignin peroxidase compound III (LiPIII) was prepared via three procedures: (a) ferrous LiP + O2 (LiPIIIa), (b) ferric LiP + 0; (LiPIIIb), and (c) LiP compound II + excess HzOz followed by treatment with catalase (LiPIIIc). LiPIIIa, h, and c each have a Soret maximum at -414 nm and visible hands at 543 and 578 nm. LiPIIIa, b, and c each slowly reverted to native ferric Lip, releasing stoichiomet...

Crystal structure of lignin peroxidase.

The crystal structure of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 A resolution by usine multiple isomorphous replacement methods and simulated annealing refinement. Of the 343 residues, residues 3-335 have been accounted for in the electron density map, including four disulfide bonds. The overall three-dimensional structure is very si...

Periodic absorption in monoclinic crystals

On the interaction of lignin peroxidase with lignin

The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer is discussed. Veratryl alcohol (Valc), a secondary metabolite of white rot fungi, acts as a cofactor for the enzyme. The Lip-redox cycle is discussed in terms of Marcus theory of electron transfer. It is proposed that reaction of a nucleophile in the active site channel with the incipient Valc'. is an essential eve...