K PAHAN

S RAY

R GACHHUI

J CHAUDHURI

A MANDAL

University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

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The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

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It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

Effect of thiol compounds and flavins on mercury and organomercurial degrading enzymes in mercury resistant aquatic bacteria.

Bulletin of Environmental Contamination and Toxicology

Five nitrogen-fixing Azotobacter strains isolated from agricultural farms in West Bengal, India, were resistant to mercuric ion and organomercurials. Resistance of Hg-resistant bacteria to mercury compounds is mediated by the activities of mercuric reductase and organomercurial lyase in the presence of NADPH and GSH as cofactors. These bacteria showed an extended lag phase in the presence of 10-50 μmol l-1 HgCl2. Nitrogen-fixing ability of these isolates was slightly inhibited when the mercury-resistant bacterial cells were preincubated with 10 μmol l-1 HgCl2. Acetylene reduction by these bacteria was significantly inhibited (91-97%) by 50 μmol l-1 HgCl2. However, when GSH and NADPH were added to the acetylene reduction assay mixture containing 50 μmol l-1 HgCl2, only 42-50% inhibition of nitrogenase activity was observed. NADPH and GSH might have a role in suppressing the inhibition of N2-fixation in the presence of Hg compounds either by assisting Hg-detoxifying enzymes to lower Hg concentration in the assay mixture or by formation of adduct comprising Hg and GSH which is unable to inhibit nitrogen fixation.

Journal of Applied Bacteriology

Studies on the effect of mercury and organomercurial on the growth and nitrogen fixation by mercury-resistant Azotobacter strains

Bacillus pasteurii DR2, a broad-spectrum Hg-resistant bacterial strain, exhibited delayed sporulation and less mercury volatilization in the presence of mercury compounds. However, Hg-sensitive Bacillus subtilis sporulated quickly in the presence of HgCl2 and volatilized no mercury. Levels of Hg2+-reductase and organomercurial lyase in the endospores of Bacillus pasteurii DR2 were lower than those in vegetative cells © 1995 Indian Academy of Sciences.

Journal of Biosciences

Mercury detoxifying enzymes within endospores of a broad-spectrum mercury resistant Bacillus pasteurii strain DR 2

A broad spectrum mercury‐resistant organism, Bacillus pasteurii DR2, was isolated from the effluents of Durgapur Steel Plant, India. In the presence of phenylmercuric acetate or benzene the rate of glucose uptake and the level of some metabolic enzymes increased significantly. Inhibition of the glucose oxidation rate by these chemicals in lysozyme‐treated cells indicated that these compounds facilitated the transport of glucose across the cell wall and thereby stimulated growth. Copyright © 1993, Wiley Blackwell. All rights reserved

Stimulatory effect of phenylmercuric acetate and benzene on the growth of a broad spectrum mercuryâ€resistant strain of Bacillus pasteurii

Environmental Research

Characteristics of Hg-resistant bacteria isolated from Minamata Bay sediment

Molecular and General Genetics MGG

A nonconjugative mobilizable broad host range plasmid of Acinetobacter sp. that determines HgCl2 resistance

Biochemistry

Deoxyribonucleic acid sequence of a gene from the Pseudomonas transposon TN501 encoding mercuric reductase

Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide

The Journal of Biochemistry

Mechanism of Mercuric Chloride Resistance in Microorganisms

Effect of thiol compounds and flavins on mercury and organomercurial degrading enzymes in mercury resistant aquatic bacteria

Journal	Data powered by TypesetBulletin of Environmental Contamination and Toxicology
Publisher	Data powered by TypesetSpringer-Verlag
ISSN	0007-4861