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Project information
Structure, function and regulation of FerB, a broad-specificity bacterial oxidoreductase of a potential ecotechnological relevance

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Project Identification
GA525/07/1069
Project Period
1/2007 - 12/2009
Investor / Pogramme / Project type
Czech Science Foundation
  • Standard Projects
MU Faculty or unit
Faculty of Science
Keywords
NAD(P)H:acceptor oxidoreductase, flavin, chromate, bioremediation, Paracoccus denitrificans

The FerB enzyme of Paracoccus denitrificans was originally discovered by our group as an NAD(P)H-dependent oxidoreductase able to reduce ferric complexes, quinones and chromate. Given the potential of using FerB for bioremediation of chromium(VI) and possibly also other heavy metals, we now propose to undertake a systematic investigation of this enzyme by conventional biochemistry, structural and molecularbiology. The gene encoding FerB will be amplified and cloned based on 27 known N-terminal amino acid residues of the protein and the already published P. denitrificans whole genome sequence. Heterologous expression of the ferB gene is expected to yield large quantities of pure recombinant protein for studies on substrate specificity, stoichiometry of electron transfer and redox kinetics of the bound flavin coenzyme. Trials will also set out to crystallise FerB and collect diffraction data for structural analysis. Suicide vectors and triparental mating will serve for construction of mutant strains lacking FerB and reporter strains carrying ferB promoter fused to the gene for β-galactosidase. Behaviour of these strains under a variety of growth conditions should provide important information on biological functions of FerB and regulation of its activity within the cell.

Publications

Total number of publications: 8

2010

2009

2008

2007

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