Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Michael H. Gold"'
Autor:
JEFFREY K. GLENN, MICHAEL H. GOLD
Publikováno v:
Archives of biochemistry and biophysics. 726
A Mn(II)-dependent peroxidase found in the extracellular medium of ligninolytic cultures of the white rot fungus, Phanerochaete chrysosporium, was purified by DEAE-Sepharose ion-exchange chromatography, Blue Agarose chromatography, and gel filtration
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1434:356-364
Genes encoding two manganese peroxidases from the white-rot basidiomycete Dichomitus squalens were cloned and sequenced. The mnp1 and mnp2 genes encode mature proteins of 369 and 365 amino acids, respectively. The amino acids involved in peroxidase f
Publikováno v:
Applied and Environmental Microbiology. 64:569-574
Manganese peroxidase (MnP) gene expression in the lignin-degrading fungus Phanerochaete chrysosporium is regulated by nutrient nitrogen levels and by Mn(II), the substrate for the enzyme, as well as by heat shock and other factors. Reverse transcript
Publikováno v:
Journal of Biological Chemistry. 272:17574-17580
Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of MnII to MnIII. The latter, acting as a diffusible redox mediator, is capable of oxidizi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1338:1-7
The gene encoding manganese peroxidase isozyme 3 (MnP3) from the white-rot basidiomycete Phanerochaete chrysosporium was cloned and sequenced. The mnp3 gene encodes a mature protein of 357 amino acids with a 25 amino-acid signal peptide. The amino ac
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1297:139-148
Two manganese peroxidase isozymes, MnP1 and MnP2, were purified from the extracellular medium of ligninolytic cultures of Dichomitus squalens . The proteins were purified to homogeneity using DEAE-Sepharose chromatography and Mono Q fast protein liqu
Autor:
Jie Sun, Michael H. Gold, Thomas M. Loehr, M.A. Kusters-van Someren, Mary B. Mayfield, K. Kishi
Publikováno v:
Biochemistry. 35:8986-8994
A series of site-directed mutants, E35Q, E39Q, and E35Q-D179N, in the gene encoding manganese peroxidase isozyme 1 (mnp1) from Phanerochaete chrysosporium, was created by overlap extension, using the polymerase chain reaction. The mutant genes were e
Publikováno v:
Journal of Biological Chemistry. 269:32759-32767
The crystal structure of manganese peroxidase (MnP) from the lignin-degrading basidiomycetous fungus Phanerochaete chrysosporium has been solved using molecular replacement techniques and refined to R = 0.20 at 2.0 A. The overall structure is similar
Publikováno v:
Biochemistry. 33:5545-5552
We demonstrate direct oxidation of ferrocytochrome c by lignin peroxidase (LiP) from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. Steady-state kinetic data fit a peroxidase ping-pong mechanism rather than an ordered bi-bi ping-pon
Publikováno v:
Journal of Molecular Biology. 238:845-848
Manganese peroxidase from the white rot basidiomycete Phanerochaete chrysosporium has been crystallized in a form suitable for high-resolution X-ray structure determination. Crystals were grown from solutions containing 30% polyethylene glycol 8000,