English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Fluoride-dependent conversion of organic compounds mediated by manganese peroxidases in the absence of Mn2+ Ions

Ye, L., Spiteller, D., Ullrich, R., Boland, W., Nueske, J., & Diekert, G. (2010). Fluoride-dependent conversion of organic compounds mediated by manganese peroxidases in the absence of Mn2+ Ions. Biochemistry, 49(34), 7264-7271. doi:10.1021/bi100831w.

Item is

Files

show Files
hide Files
:
BOL577.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
BOL577.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Chemical Ecology, MJCO; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Ye, Lidan, Author
Spiteller, Dieter1, Author           
Ullrich, Rene, Author
Boland, Wilhelm1, Author           
Nueske, Joerg, Author
Diekert, Gabriele, Author
Affiliations:
1Department of Bioorganic Chemistry, Prof. Dr. W. Boland, MPI for Chemical Ecology, Max Planck Society, ou_24028              

Content

show
hide
Free keywords: -
 Abstract: Manganese peroxidase generally mediates the oxidation of Mn2+ to Mn3+ with H2O2 as an oxidant. Several manganese peroxidases purified from different lignin-degrading fungi were found to mediate a fluoride-dependent conversion of organic substrates such as monochlorodimedone or 2,6-dimethoxyphenol in the absence of manganese ions. Using the manganese peroxidase MnP-1 from Bjerkandera adusta strain lid I, these fluoride-dependent reactions were studied with respect to different substrates converted, reaction products, and kinetic properties to shed some light on the reaction mechanism of manganese peroxidase. The analysis of the reaction products formed from monochlorodimedone and 2,6-dimethoxyphenol showed that the substrates were oxidized rather than fluorinated. The addition of fluoride to MnP-1 resulted in altered absorption spectra, indicating a coordinative binding of fluoride or HF to the heme iron; the fluoride:heme stoichiometry was determined to be 1:1 and the K-D value to be similar to 2.5 in M at pH 3.4. The high K-D value indicates weak binding of fluoride to the heme. Fluoride appeared to act as a partially competitive inhibitor with respect to hydrogen peroxide for binding to the heme as the sixth ligand. From the findings, a putative model for the fluoride-dependent reaction was developed. The data were interpreted to indicate that changes of the reaction center of manganese peroxidase as, for example, caused by fluoride binding may lead to the oxidation of organic compounds in the absence of manganese by opening a long-range electron transfer pathway.

Details

show
hide
Language(s):
 Dates: 2010
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1021/bi100831w
Other: BOL577
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 49 (34) Sequence Number: - Start / End Page: 7264 - 7271 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103