Bacterial resistances to inorganic mercury salts and organomercurials

This publication has 61 references indexed in Scilit:

• Deletion mutant analysis of the Staphylococcus aureus plasmid pI258 mercury-resistance determinant
  Canadian Journal of Microbiology, 1991
• Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation
  Biochemistry, 1990
• Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry
  Biochemistry, 1989
• The diversity of mercury reductases among mercury‐resistant bacteria
  FEBS Letters, 1988
• The Genetics and Biochemistry of Mercury Resistance
  CRC Critical Reviews in Microbiology, 1987
• Mechanistic studies of a protonolytic organomercurial cleaving enzyme: bacterial organomercurial lyase
  Biochemistry, 1986
• Bacterial organomercurial lyase: overproduction, isolation, and characterization
  Biochemistry, 1986
• The nucleotide sequence of the mercuric resistance operons of plasmid R100 and transposon Tn501: further evidence for mer genes which enhance the activity of the mercuric ion detoxification system
  Molecular Genetics and Genomics, 1986
• Deoxyribonucleic acid sequence of a gene from the Pseudomonas transposon TN501 encoding mercuric reductase
  Biochemistry, 1983
• Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide
  Biochemistry, 1983