Literature DB >> 24419943

Studies on the mercury volatilizing enzymes in nitrogen-fixing Beijerinckia mobilis.

S Ray1, K Pahan, R Gachhui, J Chaudhuri, A Mandal.   

Abstract

Beijerinckia mobilis KDr2, a broad-spectrum, mercury-resistant nitrogen-fixing organism, possesses multiple metal-resistance properties. Mercuric reductase and organomercurial lyase activities of this bacterial strain were determined using different mercury compounds and heavy metal salts of copper, nickel, cobalt, cadmium, silver, zinc, lead and arsenate as inducers and substrates. Mercuric reductase was partially purified and the effect of some enzyme inhibitors and heavy metal ions on the enzyme activity was studied. The enzyme activity was completely inhibited by CdCl2, Bi(NO3)3 and KCN at 10(-5) M and by AgNO3, CoCl2 and CuSO4 at 10(-4) M.

Entities:  

Year:  1993        PMID: 24419943     DOI: 10.1007/BF00327833

Source DB:  PubMed          Journal:  World J Microbiol Biotechnol        ISSN: 0959-3993            Impact factor:   3.312


  9 in total

1.  Purification and properties of a second enzyme catalyzing the splitting of carbon-mercury linkages from mercury-resistant Pseudomonas K-62.

Authors:  T Tezuka; K Tonomura
Journal:  J Bacteriol       Date:  1978-07       Impact factor: 3.490

Review 2.  Microbial transformations of metals.

Authors:  A O Summers; S Silver
Journal:  Annu Rev Microbiol       Date:  1978       Impact factor: 15.500

3.  The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli.

Authors:  J L Schottel
Journal:  J Biol Chem       Date:  1978-06-25       Impact factor: 5.157

4.  Bacterial organomercurial lyase: overproduction, isolation, and characterization.

Authors:  T P Begley; A E Walts; C T Walsh
Journal:  Biochemistry       Date:  1986-11-04       Impact factor: 3.162

5.  The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex.

Authors:  T V O'Halloran; B Frantz; M K Shin; D M Ralston; J G Wright
Journal:  Cell       Date:  1989-01-13       Impact factor: 41.582

6.  Mechanism of mercuric chloride resistance in microorganisms. 3. Purification and properties of a mercuric ion reducing enzyme from Escherichia coli bearing R factor.

Authors:  K Izaki; Y Tashiro; T Funaba
Journal:  J Biochem       Date:  1974-03       Impact factor: 3.387

7.  Mechanism of mercury(II) reductase and influence of ligation on the reduction of mercury(II) by a water soluble 1,5-dihydroflavin.

Authors:  E Gopinath; T W Kaaret; T C Bruice
Journal:  Proc Natl Acad Sci U S A       Date:  1989-05       Impact factor: 11.205

8.  Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide.

Authors:  B Fox; C T Walsh
Journal:  J Biol Chem       Date:  1982-03-10       Impact factor: 5.157

9.  Cell-free mercury(II)-reducing activity in a plasmid-bearing strain of Escherichia coli.

Authors:  A O Summers; L I Sugarman
Journal:  J Bacteriol       Date:  1974-07       Impact factor: 3.490

  9 in total
  1 in total

1.  Studies on mercury-detoxicating enzymes from a broad-spectrum mercury-resistant strain of Flavobacterium rigense.

Authors:  R Gachhui; J Chaudhuri; S Ray; K Pahan; A Mandal
Journal:  Folia Microbiol (Praha)       Date:  1997       Impact factor: 2.099

  1 in total

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