The genetic organization of Desulfovibrio desulphuricans ATCC 27774 bacterioferritin and rubredoxin‐2 genes: involvement of rubredoxin in iron metabolism
- 1 July 2001
- journal article
- Published by Wiley in Molecular Microbiology
- Vol. 41 (1) , 217-227
- https://doi.org/10.1046/j.1365-2958.2001.02509.x
Abstract
The anaerobic bacterium Desulfovibrio desulphuricans ATCC 27774 contains a unique bacterioferritin, isolated with a stable di‐iron centre and having iron‐coproporphyrin III as its haem cofactor, as well as a type 2 rubredoxin with an unusual spacing of four amino acid residues between the first two binding cysteines. The genes encoding for these two proteins were cloned and sequenced. The deduced amino acid sequence of the bacterioferritin shows that it is among the most divergent members of this protein family. Most interestingly, the bacterioferritin and rubredoxin‐2 genes form a dicistronic operon, which reflects the direct interaction between the two proteins. Indeed, bacterioferritin and rubredoxin‐2 form a complex in vitro, as shown by the significant increase in the anisotropy and decay times of the fluorescence of rubredoxin‐2 tryptophan(s) when mixed with bacterioferritin. In addition, rubredoxin‐2 donates electrons to bacterioferritin. This is the first identification of an electron donor to a bacterioferritin and shows the involvement of rubredoxin‐2 in iron metabolism. Furthermore, analysis of the genomic data for anaerobes suggests that rubredoxins play a general role in iron metabolism and oxygen detoxification in these prokaryotes.Keywords
This publication has 48 references indexed in Scilit:
- A Bacterioferritin from the Strict Anaerobe Desulfovibrio desulfuricans ATCC 27774Biochemistry, 2000
- Identification and characterization of a eukaryotically encoded rubredoxin in a cryptomonad alga1FEBS Letters, 2000
- The ferritins: molecular properties, iron storage function and cellular regulationPublished by Elsevier ,1999
- Site-Directed Mutagenesis of Rubredoxin Reveals the Molecular Basis of Its Electron Transfer PropertiesBiochemistry, 1997
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Rubredoxin Oxidase, a New Flavo-Hemo-Protein, Is the Site of Oxygen Reduction to Water by the "Strict Anaerobe" Desulfovibrio gigasBiochemical and Biophysical Research Communications, 1993
- The primary structure of a protein containing a putative [6Fe‐6S] prismane cluster from Desulfovibrio vulgaris (Hildenborough)European Journal of Biochemistry, 1992
- Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron clusterBiochemistry, 1988
- The amino acid sequence of desulforedoxin, a new type of non heme iron protein from Desulfovibrio gigasBiochemical and Biophysical Research Communications, 1979
- A hemoprotein from azotobacter containing non-heme iron: Isolation and crystallizationBiochemical and Biophysical Research Communications, 1973