Biochemical and Biophysical Research Communications
Regular ArticleRoles of the Four Cysteine Residues in the Function of the Integral Inner Membrane Hg2+-Binding Protein, MerC☆,☆☆
References (23)
- et al.
J. Biol. Chem.
(1991) - et al.
Biochem. Biophys. Res. Comm.
(1993) Trends Biochem. Sci.
(1985)- et al.
J. Biol. Chem.
(1997) - et al.
Trends Genet.
(1994) - et al.
Anal. Biochem.
(1992) - et al.
Anal. Biochem.
(1985) - et al.
Gene
(1990) - et al.
J. Bacteriol.
(1979) - et al.
J. Bacteriol.
(1983)
J. Gen. Microbiol.
Cited by (14)
Overexpression, purification and biophysical characterisation of E. coli MerT
2015, Protein Expression and PurificationCitation Excerpt :Subsequently Hg2+ is delivered to MerA, the cytoplasmic mercuric reductase, a multi-domain enzyme that reduces Hg2+ to volatile Hg0. The mechanism of transport of Hg2+ across the bacterial membrane mediated by MerC, MerE, MerF or MerT has been well studied [8–11]. The focus of our study, MerT, is located in the inner membrane.
Understanding toxic metal-binding proteins and peptides
2017, Handbook of Metal-Microbe Interactions and BioremediationMercury
2014, RSC Metallobiology
- ☆
Abbreviations used: SDS, sodium dodecyl sulfate; TRIS-Cl, Tris-(hydroxymethyl)aminomethane hydrochloride
- ☆☆
Muller, F.
- 1
Present address: c/o J. Powlowski, Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Blvd., W., Montreal, Quebec, H3G 1M8 Canada. Fax: 514-848-2868; E-mail:[email protected].
- 2
To whom correspondence should be addressed.
- 3
Present address: Department of Surgery, University of Umeå, S-901 87 Umeå, Sweden.