Abstract
At pH 3.0 in the absence of a reducing substrate and the presence of only 20 equivalents of H2O2, lignin peroxidase (LiP) is readily converted to LiP compound III (LiPIII) (Fe(III)O- 2 - complex). LiPIII which is produced via the reaction of LiP compound II (LiPII) with H2O2 is not part of the peroxidase catalytic cycle, and is readily and irreversibly inactivated. Veratryl alcohol (VA), a Phanerochaete chrysosporium secondary metabolite, protects the enzyme from inactivation via two mechanisms. Acting as a substrate, VA reduces LiPII to regenerate the native enzyme. Secondly, the binding of VA to LiPIII rapidly displaces O.- 2/HO.- 2, thereby converting LiPIII directly to the native enzyme. VA is not consumed during this displacement reaction. These results help to explain the role of VA in stabilizing the enzyme in the presence of excess H2O2.
| Original language | English |
|---|---|
| Pages (from-to) | 165-168 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 243 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jan 30 1989 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Lignin peroxidase compound III. Formation, inactivation, and conversion to the native enzyme. / Wariishi, Hiroyuki; Gold, Michael H.
In: FEBS Letters, Vol. 243, No. 2, 30.01.1989, p. 165-168.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Lignin peroxidase compound III. Formation, inactivation, and conversion to the native enzyme
AU - Wariishi, Hiroyuki
AU - Gold, Michael H.
PY - 1989/1/30
Y1 - 1989/1/30
N2 - At pH 3.0 in the absence of a reducing substrate and the presence of only 20 equivalents of H2O2, lignin peroxidase (LiP) is readily converted to LiP compound III (LiPIII) (Fe(III)O- 2 - complex). LiPIII which is produced via the reaction of LiP compound II (LiPII) with H2O2 is not part of the peroxidase catalytic cycle, and is readily and irreversibly inactivated. Veratryl alcohol (VA), a Phanerochaete chrysosporium secondary metabolite, protects the enzyme from inactivation via two mechanisms. Acting as a substrate, VA reduces LiPII to regenerate the native enzyme. Secondly, the binding of VA to LiPIII rapidly displaces O.- 2/HO.- 2, thereby converting LiPIII directly to the native enzyme. VA is not consumed during this displacement reaction. These results help to explain the role of VA in stabilizing the enzyme in the presence of excess H2O2.
AB - At pH 3.0 in the absence of a reducing substrate and the presence of only 20 equivalents of H2O2, lignin peroxidase (LiP) is readily converted to LiP compound III (LiPIII) (Fe(III)O- 2 - complex). LiPIII which is produced via the reaction of LiP compound II (LiPII) with H2O2 is not part of the peroxidase catalytic cycle, and is readily and irreversibly inactivated. Veratryl alcohol (VA), a Phanerochaete chrysosporium secondary metabolite, protects the enzyme from inactivation via two mechanisms. Acting as a substrate, VA reduces LiPII to regenerate the native enzyme. Secondly, the binding of VA to LiPIII rapidly displaces O.- 2/HO.- 2, thereby converting LiPIII directly to the native enzyme. VA is not consumed during this displacement reaction. These results help to explain the role of VA in stabilizing the enzyme in the presence of excess H2O2.
UR - http://www.scopus.com/inward/record.url?scp=0000608683&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0000608683&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(89)80122-X
DO - 10.1016/0014-5793(89)80122-X
M3 - Article
AN - SCOPUS:0000608683
VL - 243
SP - 165
EP - 168
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -