Journal article
A bacterial flavin reductase system reduces chromate to a soluble chromium(III)–NAD + complex
Biochemical and biophysical research communications, Vol.294(1), pp.76-81
2002
Handle:
https://hdl.handle.net/2376/105205
PMID: 12054743
Abstract
Biological reduction of carcinogenic chromate has been extensively studied in eukaryotic cells partly because the reduction produces stable chromium(III)-DNA adducts, which are mutagenic. Microbial reduction of chromate has been studied for bioremediation purposes, but little is known about the reduction mechanism. In eukaryotic cells chromate is mainly reduced non-enzymatically by ascorbate, which is usually absent in bacterial cells. We have characterized the reduction of chromate by a flavin reductase (Fre) from
Escherichia coli with flavins. The Fre-flavin system rapidly reduced chromate, whereas chemical reduction by NADH and glutathione was very slow. Thus, enzymatic chromate reduction is likely the dominant mechanism in bacterial cells. Furthermore, the end-product was a soluble and stable Cr(III)–NAD
+ complex, instead of Cr(III) precipitate. Since intracellularly generated Cr(III) forms adducts with DNA, protein, glutathione, and ascorbate in eukaryotic cells, we suggest that the produced Cr(III) is primarily complexed to NAD
+, DNA, and other cellular components inside bacteria.
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Details
- Title
- A bacterial flavin reductase system reduces chromate to a soluble chromium(III)–NAD + complex
- Creators
- Geoffrey J Puzon - School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4234, USAJames N Petersen - Center for Multiphase Environmental Research, Washington State University, Pullman, WA 99164-4234, USAArthur G Roberts - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-4234, USADavid M Kramer - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-4234, USALuying Xun - School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4234, USA
- Publication Details
- Biochemical and biophysical research communications, Vol.294(1), pp.76-81
- Academic Unit
- Chemical Engineering and Bioengineering, School of; Molecular Biosciences, School of
- Publisher
- Elsevier Inc
- Identifiers
- 99900546809001842
- Language
- English
- Resource Type
- Journal article