Ferric reductase activity of the ArsH protein from acidithiobacillus ferrooxidans

Journal of Microbiology and Biotechnology

Volumn 21, Issue 5, 2011, Pages 464-469

  Mo, Hongyu ^a,b   Chen, Qian ^a,b   Du, Juan ^a   Tang, Lin ^a   Qin, Fang ^a   Miao, Bo ^b   Wu, Xueling ^b   Zeng, Jia ^a,b  

^a HUNAN UNIVERSITY   (China)

^b CENTRAL SOUTH UNIVERSITY   (China)

Author keywords

Acidithiobacillus ferrooxidans; ArsH; Ferric reductase; Flavoprotein

Indexed keywords

BACTERIAL PROTEIN; FERRIC ION; FLAVINE MONONUCLEOTIDE REDUCTASE; IRON REDUCTASE; OXIDOREDUCTASE; PROTEIN ARSH; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ACIDITHIOBACILLUS FERROOXIDANS; ARSH GENE; ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME SPECIFICITY; ENZYME STABILITY; IRON METABOLISM; NONHUMAN; ORGANISMS BY ELECTRON DONOR; POLYMERASE CHAIN REACTION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SEQUENCE ALIGNMENT; WILD TYPE;

ACIDITHIOBACILLUS; AMINO ACID MOTIFS; BACTERIAL PROTEINS; ENZYME STABILITY; FMN REDUCTASE;

ACIDITHIOBACILLUS FERROOXIDANS; EUKARYOTA;

EID: 79958035510     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1101.01020     Document Type: Article

References (19)

1. Agarwal, R., J. B. Bonanno, S. K. Burley, and S. Swaminathan 2006. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal. Acta Cryst. D62: 383-391.
2. Butcher, B. G., S. M. Deane, and D. E. Rawlings. 2000. The chromosomal arsenic resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenic and antimony resistance to Escherichia coli. Appl. Environ. Microbiol. 66: 1826-1833.
3. Butcher, B. G. and D. E. Rawlings. 2002. The divergent chromosomal ars operon of Acidithiobacillus ferrooxidans is regulated by an atypical ArsR protein. Microbiology 148: 3983-3992.
4. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
5. Coves, J. and M. Fontecave. 1993. Reduction and mobilization of iron by a NAD(P)H:flavin oxidoreductase from Escherichia coli. Eur. J. Biochem. 211: 635-641.
6. Dancis, A., D. G. Roman, G. J. Anderson, A. G. Hinnebusch, and R. D. Klauser. 1992. Ferric reductase of Saccharomyces cerevisiae: Molecular characterization, role in iron uptake, and transcriptional control by iron. Proc. Natl. Acad. Sci. USA 89: 3869-3873.
7. Filisetti, L., J. Valton, M. Fontecave, and V. Niviere. 2005. The flavin reductase ActVB from Streptomyces coelicolor: Characterization of the electron transferase activity of the flavoprotein form. FEBS Lett. 579: 2817-2820.
8. Lopez-Maury, L., F. J. Florencio, and J. C. Reyes. 2003. Arsenic sensing and resistance system in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 185: 5363-5371.
9. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
10. Liger, D., M. Graille, C. Z. Zhou, N. Leulliot, S. Quevillon-Cheruel, K. Blondeau, J. Janin, and H. van Tilbeurgh. 2004. Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J. Biol. Chem. 279: 34890-34897.
11. Mukhopadhyay, R., B. P. Rosen, L. T. Phung, and S. Silver. 2002. Microbial arsenic: From geocycles to genes and enzymes. FEMS Microbiol. Rev. 26: 311-325.
12. Neyt, C., M. Iriarte, V. H. Thi, and G. R. Cornelis. 1997. Virulence and arsenic resistance in Yersinia. J. Bacteriol. 179: 612-619.
13. Rosen, B. P. 1999. Families of arsenic transporters. Trends Microbiol. 7: 207-212.
14. Silver, S. and L. T. Phung. 2005. Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic. Appl. Environ. Microbiol. 71: 599-608.
15. Shatwell, K. P., A. Dancis, A. R. Cross, R. D. Klausner, and A. W. Segal. 1996. The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b similar to that of NADPH oxidase. J. Biol. Chem. 271: 14240-14244.
16. Vorontsov, I. I., G. Minasov, J. S. Brunzelle, L. Shuvalova, O. Kiryukhina, F. R. Collart, and W. F. Anderson. 2007. Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity. Protein Sci. 16: 2483-2490.
17. Vadas, A., H. G. Monbouquette, E. Johnson, and I. Schröder. 1999. Identification and characterization of a novel ferric reductase from the hyperthermophilic Archaeon Archaeoglobus fulgidus. J. Biol. Chem. 274: 36715-36721.
18. Yang, H. C., J. Cheng, T. M. Finan, B. P. Rosen, and H. Bhattacharjee. 2005. Novel pathway for arsenic detoxification in the legume symbiont Sinorhizobium meliloti. J. Bacteriol. 187: 6991-6997.
19. Ye, J., H. Yang, B. P. Rosen, and H. Bhattacharjee. 2007. Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti. FEBS Lett. 581: 3996-4000.