Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview. Hg(II) removal from MerB by the N-terminal domain, NmerA, and catalytic core C-terminal cysteine pairs of its coevolved MerA and by GSH, the major competing cellular thiol in gamma-proteobacteria. The reaction with a 10fold excess of NmerA over HgMerB removes about 92% of Hg(II), while similar extents of reaction require more than 1000fold excess of GSH
evolution
MerA is part of the disulfide oxidoreductase (DSOR) family, are ancient enzymes that have arisen in high temperature environments after the great oxidation event about 2.4 billion years ago
evolution
-
MerA is part of the disulfide oxidoreductase (DSOR) family, are ancient enzymes that have arisen in high temperature environments after the great oxidation event about 2.4 billion years ago
-
physiological function
MerA catalyzes the bioconversion of toxic Hg2+ to the least toxic elemental Hg0
physiological function
organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview. Hg(II) removal from MerB by the N-terminal domain, NmerA, and catalytic core C-terminal cysteine pairs of its coevolved MerA and by GSH, the major competing cellular thiol in gamma-proteobacteria. The reaction with a 10fold excess of NmerA over HgMerB removes about 92% of Hg(II), while similar extents of reaction require more than 1000fold excess of GSH. NmerA reacts more completely than GSH with HgMerB
physiological function
the mercuric reductase is functional in high salt, stable at high temperatures, resistant to high concentrations of Hg2, and efficiently detoxifies Hg2 in vivo. Mercuric ion reductase catalyzes the reduction of Hg2+ to Hg0, which is volatile and can be disposed of nonenzymatically
physiological function
-
the enzyme catalyzes the reduction and detoxification of toxic mercuric ion, it reduces the Hg(II) ion to the less toxic elemental mercury (Hg(0)) using NADPH as a source of reducing power
additional information
-
comparison of structural changes upon metal binding in normally appended metal binding proteins: NmerA with and without Hg2+ , PDB entry 2KT3 and 2KT2, respectively
additional information
-
MerA is an inducible NADPH-dependent and flavin containing disulfide oxidoreductase enzyme. MerA-encoding plasmid R100-containing Escherichia coli strains are involved in environmental inorganic mercury detoxification
additional information
-
many MerA proteins possess metallochaperone-like N-terminal domains (NmerA) that can transfer Hg2+ to the catalytic core domain (Core) for reduction to Hg0. These domains are tethered to the homodimeric core by an about 30-residue linkers that are susceptible to proteolysis, interactions of NmerA and the Core in the full-length protein, structure homology modelling amd structure-function analysis, detailed overview. Binding of Hg2+ to MerA does not alter its hydrodynamic volume
additional information
strain R1-1 is resistant to concentration of over 0.01 mM Hg2+, transforms Hg(II) to Hg(0) during cellular growth, and possesses Hg-dependent NAD(P)H oxidation activities in crude cell extracts that are optimal at temperatures corresponding with the strains' optimal growth temperature of 70°C
additional information
the two acidic residues immediately adjacent to the NmerA metal-binding motif in the ATII-LCL protein have a direct effect on both the halophilicity and catalytic efficiency of the enzyme. Presumably, by increasing the efficiency of delivery of Hg2 ions to the catalytic core for reduction, they also help the host to cope with the high concentrations of mercury present in its hypersaline environment
additional information
-
full-length MerA homodimer structure and transfer of Hg(II) from the solvent into the catalytic sites of the MerA core, overview. Enzyme structure-function analysis by molecular dynamics, coarse-grained simulations, small-angle neutron scattering, neutron spin-echo spectroscopy, and dynamic light scattering
additional information
-
molecular mechanism of the Hg transfer is analyzed by quantum mechanical/molecular mechanical (QM/MM) calculations. The transfer is nearly thermoneutral and passes through a stable tricoordinated intermediate that is marginally less stable than the two end states. For the overall process, Hg2+ is always paired with at least two thiolates and thus is present at both the C-terminal and catalytic binding sites as a neutral complex. Prior to Hg2+ transfer, C141 is negatively charged. As Hg2+ is transferred into the catalytic site, a proton is transferred from C136 to C559' while C558' becomes negatively charged, resulting in the net transfer of a negative charge over a distance of about 7.5 A. Thus, the transport of this soft divalent cation is made energetically feasible by pairing a competition between multiple Cys thiols and/or thiolates for Hg2+ with a competition between the Hg2+ and protons for the thiolates. Reaction mechansim, formation of a tri-coordinated intermediate state, INT-III, detailed overview
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
additional information
-
the resonance Raman (RR) spectra of various functional forms of MerA are indicative of a modulation of both ring II distortion and H-bonding states of the N5 site and ring III. The Cd(II) binding to the EH2-NADP(H) complexes, biomimetic intermediates in the reaction of Hg(II) reduction, provokes important spectral changes. They are interpreted in terms of flattening of the isoalloxazine ring and large decreases in H-bonding at the N5 site and ring III. The large flexibility of the FAD structure and environment in MerA is in agreement with proposed mechanisms involving C4a(flavin) adducts
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
-
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
-
additional information
-
the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cloned and expressed constitutively in Escherichia coli
-
expression in Escherichia coli
gene merA and mer operon, expression of MerA catalytic core and NmerA proteins in Escherichia coli strain XL-1 Blue
gene merA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene merA, DNA and amino acid sequence determination and analysis, pylogenetic analysis and tree, recombinant expression in Escherichia coli strain BL21(DE3)
gene merA, expression as wild-type and mutant N-terminally His6-tagged and maltose-binding protein fusion proteins with a 3C protease cleavage site in Escherichia coli strain TOP10 and C43
-
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, mer operon located on Tn5041, DNA and amino acid sequence determination and analysis, chromosomal localization, real-time PCR enzyme expression analysis
-
gene merA, overexpression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene merA, recombinant expression in Escherichia coli strain CM037 harbouring the Tn4378 transposon which contains a mer operon of Rm CH34
-
gene merA, recombinant expression in transgenoc Nicotiana tabacum cv. Xanthium plants using gene transfer by Agrobacterium tumefaciens. Transgenic tobacco expressing merA volatilizes significantly more mercury than wild-type plants. Subcloning in Escherichia coli strains DH5alpha and BL21(DE3)
gene merA, the MerA protein is encoded by the mer operon on transposon Tn501, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene Msed_1241, phylogenetic analysis and tree, recombinant expression of codon-optimized His-tagged enzyme in Escherichia coli strain BL21(DE3)
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
plasmid transfer to mercury sensitive Escherichia coli strain DH5alpha, overexpression of gene merA as His-tagged protein in Escherichia coli BL21(DE3)Plys cells
-
recombinant expression in Escherichia coli strain BL21(DE3) pLysS
-
subcloning and expression in strain TG2, bacterial two hybrid assays are performed in strain BTH101
-
expression in Escherichia coli
-
expression in Escherichia coli
-
gene merA
-
gene merA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene merA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
gene merA, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
-
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
-
merA, DNA and amino acid sequence determination of genes from bacteria isolated from surface and sub-surface floodplain soil, phylogenetic analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Gachhui, R.; Chaudhuri, J.; Ray, S.; Pahan, K.; Mandal, A.
Studies on mercury-detoxicating enzymes from a broad-spectrum mercury-resistant strain of Flavobacterium rigense
Folia Microbiol. (Praha)
42
337-343
1997
Flavobacterium rigense, Flavobacterium rigense PR2
brenda
Fox, B.; Walsh, C.T.
Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide
J. Biol. Chem.
257
2498-2503
1982
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501
brenda
Rinderle, S.J.; Booth, J.E.; Williams, J.W.
Mercuric reductase from R-plasmid NR1: characterization and mechanistic study
Biochemistry
22
869-876
1983
Escherichia coli
brenda
Kusano, T.; Ji, G.; Inoue, C.; Silver, S.
Constitutive synthesis of a transport function encoded by the Thiobacillus ferrooxidans merC gene cloned in Escherichia coli
J. Bacteriol.
172
2688-2692
1990
Acidithiobacillus ferrooxidans
brenda
Barkay, T.; Gillman, M.; Liebert, C.
Genes encoding mercuric reductases from selected gram-negative aquatic bacteria have a low degree of homology with merA of transposon Tn501
Appl. Environ. Microbiol.
56
1695-1701
1990
Burkholderia cepacia, Pseudomonas aeruginosa, Pseudomonas stutzeri
brenda
Moore, M.J.; Distefano, M.D.; Walsh, C.T.; Schiering, N.; Pai, E.F.
Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607
J. Biol. Chem.
264
14386-14388
1989
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) RC607
brenda
Tezuka, T.; Someya, J.
Purification and some properties of mercuric reductase from the organomercury-resistant Penicillium sp. MR-2 strain
Agric. Biol. Chem.
54
1551-1552
1990
Penicillium sp., Penicillium sp. MR-2
-
brenda
Olson, G.J.; Porter, F.D.; Rubinstein, J.; Silver, S.
Mercuric reductase enzyme from a mercury-volatilizing strain of Thiobacillus ferrooxidans
J. Bacteriol.
151
1230-1236
1982
Acidithiobacillus ferrooxidans
brenda
Sahlman, L.; Lambeir, A.M.; Lindskog, S.; Dunford, H.B.
The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa
J. Biol. Chem.
259
12403-12408
1984
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501 (pVS1)
brenda
Sahlman, L.; Lindskog, S.
A stopped-flow study of the reaction between mercuric reductase and NADPH
Biochem. Biophys. Res. Commun.
117
231-237
1983
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501
brenda
Bogdanova, E.S.; Mindlin, S.Z.
Two structural types of mercury reductases and possible ways of their evolution
FEBS Lett.
247
333-336
1989
Arthrobacter sp., Priestia megaterium, Bacillus licheniformis, Paenibacillus polymyxa, Bacillus sp. (in: Bacteria), Lysinibacillus sphaericus, Citrobacter sp., Escherichia coli, Micrococcus luteus, Staphylococcus aureus, Kocuria rosea, Mycobacterium sp., Oerskovia sp., Rhodococcus sp., Staphylococcus saprophyticus
brenda
Sandstroem, A.; Lindskog, S.
Activation of mercuric reductase by the substrate NADPH
Eur. J. Biochem.
164
243-249
1987
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO 9501
brenda
Miller, S.M.; Ballou, D.P.; Massey, V.; Williams, C.H.; Walsh, C.T.
Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction
J. Biol. Chem.
261
8081-8084
1986
Escherichia coli
brenda
Nakahara, H.; Schottel, J.L.; Yamada, T.; Miyakawa, Y.; Asakawa, M.; Harville, J.; Silver, S.
Mercuric reductase enzymes from Streptomyces species and group B Streptococcus
J. Gen. Microbiol.
131
1053-1059
1985
Streptococcus agalactiae, Streptomyces coelicolor, Streptomyces espinosus, Streptomyces lividans, Streptomyces lividans 1326, Streptomyces coelicolor M130, Streptomyces espinosus 5, Streptomyces lividans 8
brenda
Booth, J.E.; Williams, J.W.
The isolation of a mercuric ion-reducing flavoprotein from Thiobacillus ferrooxidans
J. Gen. Microbiol.
130
725-730
1984
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans TFI 29
brenda
Meissner, P.S.; Falkinham, J.O.
Plasmid-encoded mercuric reductase in Mycobacterium scrofulaceum
J. Bacteriol.
157
669-672
1984
Mycobacterium scrofulaceum
brenda
Blaghen, M.; Lett, M.C.; Vidon, D.J.M.
Mercuric reductase activity in a mercury-resistant strain of Yersinia enterolytica
FEMS Microbiol. Lett.
19
93-96
1983
Yersinia enterolytica, Yersinia enterolytica 138A14
-
brenda
Carlberg, I.C.; Sahlman, L.; Mannervik, B.
The effect of 2,4,6-trinitrobenzenesulfonate on mercuric reductase, glutathione reductase and lipoamide dehydrogenase
FEBS Lett.
180
102-106
1985
Escherichia coli, Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO9501, Pseudomonas aeruginosa PAO 9501
brenda
Bogdanova, E.S.; Mindlin, S.Z.; Kalyaeva, E.S.; Nikiforov, V.G.
The diversity of mercury reductases among mercury-resistant bacteria
FEBS Lett.
234
280-282
1988
Acinetobacter calcoaceticus, Acinetobacter lwoffii, Aeromonas sp., Geobacillus stearothermophilus, Bacillus licheniformis, Paenibacillus polymyxa, Bacillus sp. (in: Bacteria), Lysinibacillus sphaericus, Escherichia coli, Erwinia sp., Staphylococcus aureus, Kocuria rosea, Oerskovia sp., Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas alcaligenes, Pseudomonas fluorescens, Pseudomonas mendocina, Rhodococcus sp., Staphylococcus saprophyticus, Xanthomonas campestris, Xanthomonas sp.
brenda
Fox, B.S.; Walsh, C.T.
Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide
Biochemistry
22
4082-4088
1983
Pseudomonas aeruginosa
brenda
Sahlman, L.; Lambeir, A.M.; Lindskog, S.
Rapid-scan stopped-flow studies of the pH dependence of the reaction between mercuric reductase and NADPH
Eur. J. Biochem.
156
479-488
1986
Pseudomonas aeruginosa
brenda
Inoue, C.; Sugawara, K.; Shiratori, T.; Kusano, T.; Kitagawa, Y.
Nucleotide sequence of the Thiobacillus ferrooxidans chromosomal gene encoding mercuric reductase
Gene
84
47-54
1989
Acidithiobacillus ferrooxidans
brenda
Rennex, D.; Pickett, M.; Bradley, M.
In vivo and in vitro effects of mutagenesis of active site tyrosine residues of mercuric reductase
FEBS Lett.
355
220-222
1994
Escherichia coli
brenda
Anspach, F.B.; Hueckel, M.; Brunke, M.; Schuette, H.; Deckwer, W.D.
Immobilization of mercuric reductase from a Pseudomonas putida strain on different activated carriers
Appl. Biochem. Biotechnol.
44
135-150
1994
Pseudomonas putida, Pseudomonas putida KT2442::mer-73
-
brenda
Blaghen, M.; Vidon, D.J.M.; El Kebbaj, M.S.
Purification and properties of mercuric reductase from Yersinia enterocolitica 138A14
Can. J. Microbiol.
39
193-200
1993
Yersinia enterolytica, Yersinia enterolytica 138A14
brenda
Ghosh, S.; Sadhukhan, P.C.; Chaudhuri, J.; Ghosh, D.K.; Mandal, A.
Purification and properties of mercuric reductase from Azotobacter chroococcum
J. Appl. Microbiol.
86
7-12
1999
Azotobacter chroococcum, Azotobacter chroococcum SS2
-
brenda
Moore, M.J.; Miller, S.M.; Walsh, C.T.
C-Terminal cysteines of Tn501 mercuric ion reductase
Biochemistry
31
1677-1685
1992
Escherichia coli
brenda
Engst, S.; Miller, S.M.
Alternative Routes for Entry of HgX2 into the Active Site of Mercuric Ion Reductase Depend on the Nature of the X Ligands
Biochemistry
38
3519-3529
1999
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) RC607
brenda
Chang, J.S.; Hwang, Y.P.; Fong, Y.M.; Lin, P.J.
Detoxification of mercury by immobilized mercuric reductase
J. Chem. Technol. Biotechnol.
74
965-973
1999
Escherichia coli, Escherichia coli PWS1
-
brenda
Rennex, D.; Cummings, R.T.; Pickett, M.; Walsh, C.T.; Bradley, M.
Role of tyrosine residues in Hg(II) detoxification by mercuric reductase from Bacillus sp. strain RC607
Biochemistry
32
7475-7478
1993
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) RC607
brenda
Zeroual, Y.; Moutaouakkil, A.; Dzairi, F.Z.; Talbi, M.; Chung, P.U.; Lee, K.; Blaghen, M.
Purification and characterization of cytosolic mercuric reductase from Klebsiella pneumoniae
Ann. Microbiol.
53
149-160
2003
Klebsiella pneumoniae
-
brenda
Vetriani, C.; Chew, Y.S.; Miller, S.M.; Yagi, J.; Coombs, J.; Lutz, R.A.; Barkay, T.
Mercury adaptation among bacteria from a deep-sea hydrothermal vent
Appl. Environ. Microbiol.
71
220-226
2005
Halomonas sp., Pseudomonas sp., Pseudoalteromonas sp., Pseudoalteromonas sp. (Q5ILH6), Alcanivorax sp., Alcanivorax sp. (Q5ILH3), Alcanivorax sp. (Q5ILH4), Alcanivorax sp. (Q5ILH5), Marinobacter sp., Alcanivorax sp. EPR 10, Alcanivorax sp. EPR 5, Alcanivorax sp. EPR 7 (Q5ILH4), Alcanivorax sp. EPR 6 (Q5ILH5), Alcanivorax sp. EPR 8 (Q5ILH3)
brenda
Kholodii, G.; Bogdanova, E.
Tn5044-conferred mercury resistance depends on temperature: the complexity of the character of thermosensitivity
Genetica
115
233-241
2002
Escherichia coli
brenda
Simbahan, J.; Kurth, E.; Schelert, J.; Dillman, A.; Moriyama, E.; Jovanovich, S.; Blum, P.
Community analysis of a mercury hot spring supports occurrence of domain-specific forms of mercuric reductase
Appl. Environ. Microbiol.
71
8836-8845
2005
uncultured bacterium
brenda
Ledwidge, R.; Patel, B.; Dong, A.; Fiedler, D.; Falkowski, M.; Zelikova, J.; Summers, A.O.; Pai, E.F.; Miller, S.M.
NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions
Biochemistry
44
11402-11416
2005
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) RC607
brenda
Schneider, M.; Deckwer, W.
Kinetics of mercury reduction by Serratia marcescens mercuric reductase expressed by Pseudomonas putida strains
Eng. Life Sci.
5
415-424
2005
Serratia marcescens
-
brenda
Schelert, J.; Dixit, V.; Hoang, V.; Simbahan, J.; Drozda, M.; Blum, P.
Occurrence and characterization of mercury resistance in the hyperthermophilic archaeon Sulfolobus solfataricus by use of gene disruption.
J. Bacteriol.
186
427-437
2004
Saccharolobus solfataricus (Q97VD9), Saccharolobus solfataricus
brenda
Schue, M.; Glendinning, K.J.; Hobman, J.L.; Brown, N.L.
Evidence for direct interactions between the mercuric ion transporter (MerT) and mercuric reductase (MerA) from the Tn501 mer operon
Biometals
21
107-116
2008
Escherichia coli K-12
brenda
Oregaard, G.; S?rensen, S.J.
High diversity of bacterial mercuric reductase genes from surface and sub-surface floodplain soil (Oak Ridge, USA)
ISME J.
1
453-467
2007
uncultured Gammaproteobacteria bacterium, Actinobacteria, uncultured beta proteobacterium
brenda
Park, S.; Ely, R.L.
Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals
Appl. Environ. Microbiol.
74
5475-5482
2008
Nitrosomonas europaea
brenda
Radniecki, T.S.; Semprini, L.; Dolan, M.E.
Expression of merA, amoA and hao in continuously cultured Nitrosomonas europaea cells exposed to zinc chloride additions
Biotechnol. Bioeng.
102
546-553
2009
Nitrosomonas europaea
brenda
Radniecki, T.S.; Semprini, L.; Dolan, M.E.
Expression of merA, trxA, amoA, and hao in continuously cultured Nitrosomonas europaea cells exposed to cadmium sulfate additions
Biotechnol. Bioeng.
104
1004-1011
2009
Nitrosomonas europaea
brenda
Zeyaullah, M.; Haque, S.; Nabi, G.; Nand, K.; Ali, A.
Molecular cloning and expression of bacterial mercuric reductase gene
Afr. J. Biotechnol.
9
3714-3718
2010
plasmid R100
-
brenda
Hong, B.; Nauss, R.; Harwood, I.M.; Miller, S.M.
Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved gamma-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione
Biochemistry
49
8187-8196
2010
Serratia marcescens (E0XF09)
brenda
Ledwidge, R.; Hong, B.; Doetsch, V.; Miller, S.M.
NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols
Biochemistry
49
8988-8998
2010
Pseudomonas aeruginosa
brenda
Haque, S.; Zeyaullah, M.; Nabi, G.; Srivastava, P.S.; Ali, A.
Transgenic tobacco plant expressing environmental E. coli merA gene for enhanced volatilization of ionic mercury
J. Microbiol. Biotechnol.
20
917-924
2010
Escherichia coli (Q93UN8), Escherichia coli
brenda
Freedman, Z.; Zhu, C.; Barkay, T.
Mercury resistance and mercuric reductase activities and expression among chemotrophic thermophilic Aquificae
Appl. Environ. Microbiol.
78
6568-6575
2012
Hydrogenivirga sp. 128-5-R1-1 (A8UT36), Hydrogenobaculum sp. Y04AAS1 (B4U9T7)
brenda
Zhang, W.; Chen, L.; Liu, D.
Characterization of a marine-isolated mercury-resistant Pseudomonas putida strain SP1 and its potential application in marine mercury reduction
Appl. Microbiol. Biotechnol.
93
1305-1314
2012
Pseudomonas putida, Pseudomonas putida SP1
brenda
Bafana, A.; Chakrabarti, T.; Krishnamurthi, K.
Mercuric reductase activity of multiple heavy metal-resistant Lysinibacillus sphaericus G1
J. Basic Microbiol.
55
285-992
2015
Lysinibacillus sphaericus (D9J041), Lysinibacillus sphaericus, Lysinibacillus sphaericus G1 (D9J041)
brenda
Sayed, A.; Ghazy, M.A.; Ferreira, A.J.; Setubal, J.C.; Chambergo, F.S.; Ouf, A.; Adel, M.; Dawe, A.S.; Archer, J.A.; Bajic, V.B.; Siam, R.; El-Dorry, H.
A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea
J. Biol. Chem.
289
1675-1687
2014
uncultured prokaryote (V5TDP2)
brenda
Johs, A.; Harwood, I.M.; Parks, J.M.; Nauss, R.E.; Smith, J.C.; Liang, L.; Miller, S.M.
Structural characterization of intramolecular Hg2+ transfer between flexibly linked domains of mercuric ion reductase
J. Mol. Biol.
413
639-656
2011
Shigella flexneri
brenda
Lian, P.; Guo, H.B.; Riccardi, D.; Dong, A.; Parks, J.M.; Xu, Q.; Pai, E.F.; Miller, S.M.; Wei, D.Q.; Smith, J.C.; Guo, H.
X-ray structure of a Hg2+ complex of mercuric reductase (MerA) and quantum mechanical/molecular mechanical study of Hg2+ transfer between the C-terminal and buried catalytic site cysteine pairs
Biochemistry
53
7211-7222
2014
Pseudomonas aeruginosa
brenda
Bafana, A.; Khan, F.; Suguna, K.
Structural and functional characterization of mercuric reductase from Lysinibacillus sphaericus strain G1
Biometals
30
809-819
2017
Lysinibacillus sphaericus (D9J041), Lysinibacillus sphaericus, Lysinibacillus sphaericus G1 (D9J041)
brenda
Hong, L.; Sharp, M.A.; Poblete, S.; Biehl, R.; Zamponi, M.; Szekely, N.; Appavou, M.S.; Winkler, R.G.; Nauss, R.E.; Johs, A.; Parks, J.M.; Yi, Z.; Cheng, X.; Liang, L.; Ohl, M.; Miller, S.M.; Richter, D.; Gompper, G.; Smith, J.C.
Structure and dynamics of a compact state of a multidomain protein, the mercuric ion reductase
Biophys. J.
107
393-400
2014
Pseudomonas aeruginosa
brenda
Keirsse-Haquin, J.; Picaud, T.; Bordes, L.; de Gracia, A.G.; Desbois, A.
Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase a resonance Raman study
Eur. Biophys. J.
47
205-223
2018
Enterococcus faecalis, Cupriavidus metallidurans
brenda
Moller, A.K.; Barkay, T.; Hansen, M.; Norman, A.; Hansen, L.; Soslas, S.; rensen, S.; Boyd, E.; Kroer, N.
Mercuric reductase genes (merA) and mercury resistance plasmids in high arctic snow, freshwater and sea-ice brine
FEMS Microbiol. Ecol.
87
52-63
2014
Variovorax sp. SOK15 (T1RLC6), Pseudomonas sp. SOK70 (T1RLC7), Arthrobacter sp. 8D5s (T1RLC8), Bacillus sp. SOK1b (T1RLH1), Flavobacterium sp. SOK62 (T1RLH3), Pseudomonas sp. SOK89 (T1RLH7), Pseudomonas sp. SOK44 (T1RLH8), Pseudomonas sp. SOK13 (T1RLH9), Pseudomonas sp. SOK52 (T1RR73), Pseudomonas sp. SOK32 (T1RR74), Pseudomonas sp. SOK80 (T1RR75), Pseudomonas sp. SOK65 (T1RR77), Pseudomonas sp. SOK54 (T1RRJ1), Sphingomonas sp. SOK19y (T1RRJ3), Pseudomonas sp. SOK75 (T1RRJ7), Pseudomonas sp. SOK59 (T1RRJ9), Sphingomonas sp. SOK19 (T1RRK0), Pseudomonas sp. SOK73 (T1RRK2), Pseudomonas sp. SOK43 (T1RRL9), Pseudomonas sp. SOK41 (T1RRM0), Sphingomonas sp. SOK5 (T1RRM1), Pseudomonas sp. SOK85 (T1RRM2), Pseudomonas sp. SOK50 (T1RRS1), Pseudomonas sp. SOK33 (T1RRS2), Pseudomonas sp. SOK84 (T1RRS3), Pseudomonas sp. SOK68 (T1RRS4)
brenda
Artz, J.H.; White, S.N.; Zadvornyy, O.A.; Fugate, C.J.; Hicks, D.; Gauss, G.H.; Posewitz, M.C.; Boyd, E.S.; Peters, J.W.
Biochemical and structural properties of a thermostable mercuric ion reductase from Metallosphaera sedula
Front. Bioeng. Biotechnol.
3
97
2015
Metallosphaera sedula (A4YG49), Metallosphaera sedula, Metallosphaera sedula ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 (A4YG49)
brenda
Giovanella, P.; Cabral, L.; Bento, F.M.; Gianello, C.; Camargo, F.A.
Mercury (II) removal by resistant bacterial isolates and mercuric (II) reductase activity in a new strain of Pseudomonas sp. B50A
New Biotechnol.
33
216-223
2016
Pseudomonas putida, Pseudomonas entomophila, Enterobacter sp. B50C, Enterobacter sp. A25B, Pseudomonas sp. B50A, Pseudomonas sp. B50B, Pseudomonas sp. B50D, Pseudomonas entomophila A50A, Pseudomonas putida V1, Pseudomonas entomophila B100A
brenda