Mercuric Reductase Enzymes from Streptomyces Species and Group B Streptococcus
- 1 May 1985
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 131 (5) , 1053-1059
- https://doi.org/10.1099/00221287-131-5-1053
Abstract
Mercury volatilization (Hg2+ reductase) activity has been found with Hg2+-resistant isolates of three Streptomyces species and with three Hg2+-resistant strains of group B Streptococcus from clinical sources in Japan. Hg2+ reductase activities in crude cell extracts showed the temperature sensitivity, the requirement for an added thiol compound and the characteristic dependence on NAD(P)H cofactors of similar enzymes isolated from other bacteria.This publication has 3 references indexed in Scilit:
- Deoxyribonucleic acid sequence of a gene from the Pseudomonas transposon TN501 encoding mercuric reductaseBiochemistry, 1983
- Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptideBiochemistry, 1983
- Tn5 insertion mutations in the mercuric ion resistance genes derived from plasmid R100Journal of Bacteriology, 1983