Affordable Access

deepdyve-link
Publisher Website

Mechanism of chlorite degradation to chloride and dioxygen by the enzyme chlorite dismutase.

Authors
  • Schaffner, Irene1
  • Hofbauer, Stefan2
  • Krutzler, Michael1
  • Pirker, Katharina F1
  • Furtmüller, Paul G1
  • Obinger, Christian3
  • 1 Department of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. , (Austria)
  • 2 Department of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria; Department for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria. , (Austria)
  • 3 Department of Chemistry, Division of Biochemistry, BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. Electronic address: [email protected] , (Austria)
Type
Published Article
Journal
Archives of Biochemistry and Biophysics
Publisher
Elsevier
Publication Date
May 15, 2015
Volume
574
Pages
18–26
Identifiers
DOI: 10.1016/j.abb.2015.02.031
PMID: 25748001
Source
Medline
Keywords
License
Unknown

Abstract

Heme b containing chlorite dismutase (Cld) catalyses the conversion of chlorite to chloride and dioxygen which includes an unusual OO bond formation. This review summarizes our knowledge about the interaction of chlorite with heme enzymes and introduces the biological role, phylogeny and structure of functional chlorite dismutases with differences in overall structure and subunit architecture. The paper sums up the available experimental and computational studies on chlorite degradation by water soluble porphyrin complexes as well as a model based on the active site of Cld. Finally, it reports the available biochemical and biophysical data of Clds from different organisms which allow the presentation of a general reaction mechanism. It includes binding of chlorite to ferric Cld followed by subsequent heterolytic OCl bond cleavage leading to the formation of Compound I and hypochlorite, which finally recombine for production of chloride and O2. The role of the Cld-typical distal arginine in catalysis is discussed together with the pH dependence of the reaction and the role of transiently produced hypochlorite in irreversible inactivation of the enzyme.

Report this publication

Statistics

Seen <100 times