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2VXH: The Crystal Structure Of Chlorite Dismutase: A Detox Enzyme Producing Molecular Oxygen
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4530992
Author(s) De Geus, D. C.; Thomassen, E. A. J.; Hagedoorn, P. L.; Pannu, N. S.; Abrahams, J. P.
Author(s) at UniBasel Abrahams, Jan Pieter
Year 2009
Title 2VXH: The Crystal Structure Of Chlorite Dismutase: A Detox Enzyme Producing Molecular Oxygen
Journal Worldwide Protein Data Bank
Pages / Article-Number 2VXH
Keywords Oxidoreductase
Mesh terms Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiochemistry & Molecular Biology
Abstract Chlorite dismutase (Cld) is a key enzyme of perchlorate and chlorate respiration. This heme-based protein reduces the toxic compound chlorite into the innocuous chloride anion in a very efficient way while producing molecular oxygen. A sequence comparison between Cld homologues shows a highly conserved family. The crystal structure of Azospira oryzae strain GR-1 Cld is reported to 2.1 A resolution. The structure reveals a hexameric organization of the Cld, while each monomer exhibits a ferredoxin-like fold. The six subunits are organized in a ring structure with a maximal diameter of 9 nm and an inner diameter of 2 nm. The heme active-site pocket is solvent accessible both from the inside and the outside of the ring. Moreover, a second anion binding site that could accommodate the assumed reaction intermediate ClO(-) for further transformation has been identified near the active site. The environment of the heme cofactor was investigated with electron paramagnetic resonance spectroscopy. Apart from the high-spin ferric signal of the five-coordinate resting-state enzyme, two low-spin signals were found corresponding to six-coordinate species. The current crystal structure confirms and complements a recently proposed catalytic mechanism that proceeds via a ferryl species and a ClO(-) anion. Our structural data exclude cooperativity between the iron centers.
edoc-URL https://edoc.unibas.ch/75928/
Full Text on edoc No
Digital Object Identifier DOI 10.2210/pdb2vxh/pdb
ISI-Number 2012140001761170
Document type (ISI) Data set
 
   

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