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The relationship between protein structural characteristics and temperature optimum for activity of the mercuric reductase from two species of bacteroidetes

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Title
The relationship between protein structural characteristics and temperature optimum for activity of the mercuric reductase from two species of bacteroidetes
Name (type = personal)
NamePart (type = family)
Manavi
NamePart (type = given)
Bahram
DisplayForm
Bahram Manavi
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Barkay
NamePart (type = given)
Tamar
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Tamar Barkay
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Kahn
NamePart (type = given)
Peter C.
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Peter C. Kahn
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Chase
NamePart (type = given)
Theodore
DisplayForm
Theodore Chase
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2014
DateOther (qualifier = exact); (type = degree)
2014-10
CopyrightDate (encoding = w3cdtf)
2014
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
During the past five decades, mercury has gained increased interest due to its toxicity to human and environmental health. Therefore, mercury detoxification, whereby the mercuric reductase (MR), a homodimer of MerA (Figure 3 10), converts Hg2+ to Hg0, is an important activity. merA, the gene encoding MerA, has been found in diverse Archaea and Bacteria [1], but it is not well known in the Bacteroidetes, a large phylum in the bacterial domain that is widely distributed in many environments. The goal of this study was to identify protein structural characteristics that relate to MerA temperature optimum for activity in two species of the phylum Bacteroidetes: one a thermophile, Rhodothermus marinus, and the other a psychrophile, Flavobacterium. sp. SOK62. The standard MerA assay [2] was optimized by adjusting pH, selecting the reducing substrates (NADH/NADPH) and the type and concentration of thiol agent. Using the optimized assay, I found that the optimum temperature for MerA of R. marinus was at 65-70˚C (activity range from 30 to 90 ºC) and for the psychrophilic MerA (strain SOK62) was at 50-55 ˚C (range from 10 to 90 ºC). Homology modeling (Figure 3 7) of the psychrophilic and thermophilic MerA (homology to a proteobacterial MerA from Pseudomonas aeruginosa PAT) showed that the psychrophile’s MerA (SOK62) has more α-helix and less β-sheet secondary structure than the thermophile’s MerA (R. marinus), which is shown in Table 3 5. MerA of SOK62 has more polar residues and less hydrophobic residues, suggesting adaptation to activity at lower temperatures [3]than MerA of R. marinus. In contrast, the psychrophile’s MerA has a larger number of aromatic residues than the R. marinus enzyme, contradicting the expectation of a lower number of bulky residues in a psychrophilic protein. These experiments test the hypothesis that because MerA originated among thermophiles in geothermal environments [4], the MerA from a psychrophilic bacterium has a thermophilic enzyme activity optimum and structural adaptations facilitating activity at low temperatures. This study contributes to our understanding of the natural history of microbial mercury detoxification.
Subject (authority = RUETD)
Topic
Microbial Biology
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_5858
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Note
Supplementary File: Reprint Permission for Figure 1.2
Extent
1 online resource (xiv, 50 p. : ill.)
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Subject (authority = ETD-LCSH)
Topic
Mercury--Toxicology
Subject (authority = ETD-LCSH)
Topic
Bacteriology
Note (type = statement of responsibility)
by Bahram Manavi
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
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NjNbRU
Identifier (type = doi)
doi:10.7282/T3QZ28NV
Genre (authority = ExL-Esploro)
ETD graduate
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The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Manavi
GivenName
Bahram
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2014-09-18 22:14:35
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Bahram Manavi
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Affiliation
Rutgers University. Graduate School - New Brunswick
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Author Agreement License
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I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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Copyright protected
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Open
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Permission or license
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