NDLI: Mercury(II) complex formation with glutathione in alkaline aqueous solution

Please wait, while we are loading the content...

Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial Complexes II and III and related proteins

Structural and spectroscopic studies of a model for catechol oxidase

Ruthenium(III) dimethyl sulfoxide pyridinehydroxamic acid complexes as potential antimetastatic agents: synthesis, characterisation and in vitro pharmacological evaluation

QM/MM theoretical study of the pentacoordinate Mn(III) and resting states of manganese-reconstituted cytochrome P450cam

Modulation of NO binding to cytochrome c′ by distal and proximal haem pocket residues

Mercury(II) complex formation with glutathione in alkaline aqueous solution

Inhibition of cathepsin B by Au(I) complexes: a kinetic and computational study

Spectroscopic evidence for an all-ferrous [4Fe–4S]0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans

DNA cleavage and binding selectivity of a heterodinuclear Pt–Cu(3-Clip-Phen) complex

One of the possible mechanisms for the inhibition effect of Tb(III) on peroxidase activity in horseradish (Armoracia rusticana) treated with Tb(III)

Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants

Ambidentate H-bonding by heme-bound NO: structural and spectral effects of –O versus –N H-bonding

Structural basis for VO2+ inhibition of nitrogenase activity (A): 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy

Structural basis for VO2+-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe–protein identified by ENDOR spectroscopy

Structural basis for VO2+ inhibition of nitrogenase activity: (A) 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy

A note from the President

JBIC Journal of Biological Inorganic Chemistry : Volume 13, Issue 3, March 2008

JBIC Journal of Biological Inorganic Chemistry : Volume 13, Issue 2, February 2008

JBIC Journal of Biological Inorganic Chemistry : Volume 13, Issue 1, January 2008

JBIC Journal of Biological Inorganic Chemistry : Volume 12

JBIC Journal of Biological Inorganic Chemistry : Volume 11

JBIC Journal of Biological Inorganic Chemistry : Volume 10

JBIC Journal of Biological Inorganic Chemistry : Volume 9

JBIC Journal of Biological Inorganic Chemistry : Volume 8

JBIC Journal of Biological Inorganic Chemistry : Volume 7

JBIC Journal of Biological Inorganic Chemistry : Volume 6

JBIC Journal of Biological Inorganic Chemistry : Volume 5

JBIC Journal of Biological Inorganic Chemistry : Volume 4

JBIC Journal of Biological Inorganic Chemistry : Volume 3

JBIC Journal of Biological Inorganic Chemistry : Volume 2

Mercury(II) complex formation with glutathione in alkaline aqueous solution

Content Provider	Springer Nature Link
Author	Mah, Vicky Jalilehvand, Farideh
Copyright Year	2008
Abstract	The structure and speciation of the complexes formed between mercury(II) ions and glutathione (GSH = L-glutamyl-L-cysteinyl-glycine) have been studied for a series of alkaline aqueous solutions ( $$ C_{{{\text{Hg}}^{{2 + }}}}\,{\sim18\,{\rm{mmol}}\,{\rm{{dm^{-3}}}}}$$ and C GSH = 40–200 mmol dm−3 at pH ∼10.5) by means of extended X-ray absorption fine structure (EXAFS) and 199Hg NMR spectroscopy at ambient temperature. The dominant complexes are [Hg(GS)2]4− and [Hg(GS)3]7−, with mean Hg–S bond distances of 2.32(1) and 2.42(2) Å observed in digonal and trigonal Hg–S coordination, respectively. The proportions of the Hg2+–glutathione complexes were evaluated by fitting linear combinations of model EXAFS oscillations representing each species to the experimental EXAFS spectra. The [Hg(GS)4]10− complex, with four sulfur atoms coordinated at a mean Hg–S bond distance of 2.52(2) Å, is present in minor amounts (<30%) in solutions containing a large excess of glutathione (C GSH ≥ 160 mmol dm−3). Comparable alkaline mercury(II) cysteine (H2Cys) solutions were also investigated and a reduced tendency to form higher complexes was observed, because the deprotonated amino group of Cys2− allows the stable [Hg(S,N-Cys)2]2− chelate to form. The effect of temperature on the distribution of the Hg2+–glutathione complexes was studied by comparing the EXAFS spectra at ambient temperature and at 25 K of a series of glycerol/water (33/67, v/v) frozen glasses with $$ C_{{{\text{Hg}}^{{2 + }} }} \,{\sim7\,{\rm{mmol}}\,{\rm{{dm^{-3}}}}} $$ and C GSH = 16–81 mmol dm−3. Complexes with high Hg–S coordination numbers, [Hg(GS)3]7− and [Hg(GS)4]10−, became strongly favored when just a moderate excess of glutathione (C GSH ≥28 mmol dm−3) was used in the glassy samples, as expected for a stepwise exothermic bond formation. Addition of glycerol had no effect on the Hg(II)–glutathione speciation, as shown by the similarity of the EXAFS spectra obtained at room temperature for two parallel series of Hg(II)-glutathione solutions with $$ C_{{{\text{Hg}}^{{2 + }} }} \,{\sim7\,{\rm{mmol}}\,{\rm{{dm^{-3}}}}},$$ with and without 33% glycerol. Also, the 199Hg NMR chemical shifts of a series of ∼18 mmol dm−3 mercury(II) glutathione solutions with 33% glycerol were not significantly different from those of the corresponding series in aqueous solution.
Starting Page	541
Ending Page	553
Page Count	13
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	13
Issue Number	4
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-01-26
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Mercury(II) Glutathione Solution EXAFS 199Hg NMR Microbiology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Cadmium(II) complex formation with glutathione

Mercury(II) complex formation with glutathione in alkaline aqueous solution

Mixed complex formation of lead(II) and mercury(II) ethylenediaminetetraacetates with thiourea in an aqueous solution

Thermochemical study of the complex formation of mercury(II) with nitrilotriacetic acid in an aqueous solution

Thermodynamics of Mixed-Ligand Complex Formation of Mercury(II) Ethylenediaminetetraacetate with Ethylenediamine and Hexamethylenediamine in an Aqueous Solution

Thermodynamics of the Mixed-Ligand Complex Formation of Mercury(II) Ethylenediaminetetraacetate with Dipyridine and Phenanthroline in Aqueous Solution

Glutathione Complex Formation with Mercury(II) in Aqueous Solution at Physiological pH

Thermodynamics of complex formation of Cu(II) ethylenediaminetetraacetate with ethylenediamine in aqueous solution

Homo- and heteroleptic mercury(II) complexes with monoamino complexones in aqueous solution

Mercury(II) complex formation with glutathione in alkaline aqueous solution

Similar Documents

Cadmium(II) complex formation with glutathione

Mercury(II) complex formation with glutathione in alkaline aqueous solution

Mixed complex formation of lead(II) and mercury(II) ethylenediaminetetraacetates with thiourea in an aqueous solution

Thermochemical study of the complex formation of mercury(II) with nitrilotriacetic acid in an aqueous solution

Thermodynamics of Mixed-Ligand Complex Formation of Mercury(II) Ethylenediaminetetraacetate with Ethylenediamine and Hexamethylenediamine in an Aqueous Solution

Thermodynamics of the Mixed-Ligand Complex Formation of Mercury(II) Ethylenediaminetetraacetate with Dipyridine and Phenanthroline in Aqueous Solution

Glutathione Complex Formation with Mercury(II) in Aqueous Solution at Physiological pH

Thermodynamics of complex formation of Cu(II) ethylenediaminetetraacetate with ethylenediamine in aqueous solution

Homo- and heteroleptic mercury(II) complexes with monoamino complexones in aqueous solution

Mercury(II) complex formation with glutathione in alkaline aqueous solution