Structure of the active site of lignin peroxidase isozyme H2: Native enzyme, compound III, and reduced Form

R. Sinclair, I. Yamazaki, J. Bumpus, Linda S Powers, C. S. Chang, A. Albo, L. Powers

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The wood-degrading fungus Phanerochaete chrysosporium secretes a number of extracellular enzymes called lignin peroxidases which are involved in the degradation of both lignin and a number of persistent environmental pollutants. Lignin peroxidase isozyme H2, a glycosylated protein of approximately 40 kDa, contains a single heme. X-ray absorption spectroscopy (XAS) has been used to probe the local environment of the iron in the active site of resting enzyme, reduced enzyme, and compound III. For the native and reduced forms, respectively, the average Fe-pyrrole nitrogen distances are 2.055 and 2.02 Å (±0.015 Å); the Fe-proximal nitrogen distance is 1.93 and 1.91 A (±0.02 Å) while the Fe-distal ligand distance is 2.17 and 2.10 Å (±0.03 Å). Although the results are not as well-defined, the active-site structure of compound III is largely 2.02 ±0.015 Å for the average Fe-pyrrole nitrogen distance, 1.90 ± 0.02 for the Fe-proximal nitrogen, and 1.74 ± 0.03 Å for the Fe-distal ligand distance. The heme iron-pyrrole nitrogen distnce is more expanded in ligninase H2 than in other peroxidases. The possible significance of this is discussed in relation to other heme proteins.

Original languageEnglish (US)
Pages (from-to)4892-4900
Number of pages9
JournalBiochemistry
Volume31
Issue number20
StatePublished - 1992
Externally publishedYes

Fingerprint

Isoenzymes
Catalytic Domain
Nitrogen
Pyrroles
Enzymes
Heme
Iron
X-Ray Absorption Spectroscopy
Phanerochaete
Ligands
Hemeproteins
Peroxidases
Environmental Pollutants
X ray absorption spectroscopy
Lignin
Fungi
Wood
lignin peroxidase
Degradation
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Sinclair, R., Yamazaki, I., Bumpus, J., Powers, L. S., Chang, C. S., Albo, A., & Powers, L. (1992). Structure of the active site of lignin peroxidase isozyme H2: Native enzyme, compound III, and reduced Form. Biochemistry, 31(20), 4892-4900.

Structure of the active site of lignin peroxidase isozyme H2 : Native enzyme, compound III, and reduced Form. / Sinclair, R.; Yamazaki, I.; Bumpus, J.; Powers, Linda S; Chang, C. S.; Albo, A.; Powers, L.

In: Biochemistry, Vol. 31, No. 20, 1992, p. 4892-4900.

Research output: Contribution to journalArticle

Sinclair, R, Yamazaki, I, Bumpus, J, Powers, LS, Chang, CS, Albo, A & Powers, L 1992, 'Structure of the active site of lignin peroxidase isozyme H2: Native enzyme, compound III, and reduced Form', Biochemistry, vol. 31, no. 20, pp. 4892-4900.
Sinclair, R. ; Yamazaki, I. ; Bumpus, J. ; Powers, Linda S ; Chang, C. S. ; Albo, A. ; Powers, L. / Structure of the active site of lignin peroxidase isozyme H2 : Native enzyme, compound III, and reduced Form. In: Biochemistry. 1992 ; Vol. 31, No. 20. pp. 4892-4900.
@article{eaf63009535e4dc59342bcbc72d260bc,
title = "Structure of the active site of lignin peroxidase isozyme H2: Native enzyme, compound III, and reduced Form",
abstract = "The wood-degrading fungus Phanerochaete chrysosporium secretes a number of extracellular enzymes called lignin peroxidases which are involved in the degradation of both lignin and a number of persistent environmental pollutants. Lignin peroxidase isozyme H2, a glycosylated protein of approximately 40 kDa, contains a single heme. X-ray absorption spectroscopy (XAS) has been used to probe the local environment of the iron in the active site of resting enzyme, reduced enzyme, and compound III. For the native and reduced forms, respectively, the average Fe-pyrrole nitrogen distances are 2.055 and 2.02 {\AA} (±0.015 {\AA}); the Fe-proximal nitrogen distance is 1.93 and 1.91 A (±0.02 {\AA}) while the Fe-distal ligand distance is 2.17 and 2.10 {\AA} (±0.03 {\AA}). Although the results are not as well-defined, the active-site structure of compound III is largely 2.02 ±0.015 {\AA} for the average Fe-pyrrole nitrogen distance, 1.90 ± 0.02 for the Fe-proximal nitrogen, and 1.74 ± 0.03 {\AA} for the Fe-distal ligand distance. The heme iron-pyrrole nitrogen distnce is more expanded in ligninase H2 than in other peroxidases. The possible significance of this is discussed in relation to other heme proteins.",
author = "R. Sinclair and I. Yamazaki and J. Bumpus and Powers, {Linda S} and Chang, {C. S.} and A. Albo and L. Powers",
year = "1992",
language = "English (US)",
volume = "31",
pages = "4892--4900",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "20",

}

TY - JOUR

T1 - Structure of the active site of lignin peroxidase isozyme H2

T2 - Native enzyme, compound III, and reduced Form

AU - Sinclair, R.

AU - Yamazaki, I.

AU - Bumpus, J.

AU - Powers, Linda S

AU - Chang, C. S.

AU - Albo, A.

AU - Powers, L.

PY - 1992

Y1 - 1992

N2 - The wood-degrading fungus Phanerochaete chrysosporium secretes a number of extracellular enzymes called lignin peroxidases which are involved in the degradation of both lignin and a number of persistent environmental pollutants. Lignin peroxidase isozyme H2, a glycosylated protein of approximately 40 kDa, contains a single heme. X-ray absorption spectroscopy (XAS) has been used to probe the local environment of the iron in the active site of resting enzyme, reduced enzyme, and compound III. For the native and reduced forms, respectively, the average Fe-pyrrole nitrogen distances are 2.055 and 2.02 Å (±0.015 Å); the Fe-proximal nitrogen distance is 1.93 and 1.91 A (±0.02 Å) while the Fe-distal ligand distance is 2.17 and 2.10 Å (±0.03 Å). Although the results are not as well-defined, the active-site structure of compound III is largely 2.02 ±0.015 Å for the average Fe-pyrrole nitrogen distance, 1.90 ± 0.02 for the Fe-proximal nitrogen, and 1.74 ± 0.03 Å for the Fe-distal ligand distance. The heme iron-pyrrole nitrogen distnce is more expanded in ligninase H2 than in other peroxidases. The possible significance of this is discussed in relation to other heme proteins.

AB - The wood-degrading fungus Phanerochaete chrysosporium secretes a number of extracellular enzymes called lignin peroxidases which are involved in the degradation of both lignin and a number of persistent environmental pollutants. Lignin peroxidase isozyme H2, a glycosylated protein of approximately 40 kDa, contains a single heme. X-ray absorption spectroscopy (XAS) has been used to probe the local environment of the iron in the active site of resting enzyme, reduced enzyme, and compound III. For the native and reduced forms, respectively, the average Fe-pyrrole nitrogen distances are 2.055 and 2.02 Å (±0.015 Å); the Fe-proximal nitrogen distance is 1.93 and 1.91 A (±0.02 Å) while the Fe-distal ligand distance is 2.17 and 2.10 Å (±0.03 Å). Although the results are not as well-defined, the active-site structure of compound III is largely 2.02 ±0.015 Å for the average Fe-pyrrole nitrogen distance, 1.90 ± 0.02 for the Fe-proximal nitrogen, and 1.74 ± 0.03 Å for the Fe-distal ligand distance. The heme iron-pyrrole nitrogen distnce is more expanded in ligninase H2 than in other peroxidases. The possible significance of this is discussed in relation to other heme proteins.

UR - http://www.scopus.com/inward/record.url?scp=0026666938&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026666938&partnerID=8YFLogxK

M3 - Article

C2 - 1591249

AN - SCOPUS:0026666938

VL - 31

SP - 4892

EP - 4900

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 20

ER -