Document Detail


Sulfur K-edge x-ray absorption spectroscopy: a spectroscopic tool to examine the redox state of S-containing metabolites in vivo.
MedLine Citation:
PMID:  9600928     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The sulfur K-edge x-ray absorption spectra for the amino acids cysteine and methionine and their corresponding oxidized forms cystine and methionine sulfoxide are presented. Distinct differences in the shape of the edge and the inflection point energy for cysteine and cystine are observed. For methionine sulfoxide the inflection point energy is 2.8 eV higher compared with methionine. Glutathione, the most abundant thiol in animal cells, also has been investigated. The x-ray absorption near-edge structure spectrum of reduced glutathione resembles that of cysteine, whereas the spectrum of oxidized glutathione resembles that of cystine. The characteristic differences between the thiol and disulfide spectra enable one to determine the redox status (thiol to disulfide ratio) in intact biological systems, such as unbroken cells, where glutathione and cyst(e)ine are the two major sulfur-containing components. The sulfur K-edge spectra for whole human blood, plasma, and erythrocytes are shown. The erythrocyte sulfur K-edge spectrum is similar to that of fully reduced glutathione. Simulation of the plasma spectrum indicated 32% thiol and 68% disulfide sulfur. The whole blood spectrum can be simulated by a combination of 46% disulfide and 54% thiol sulfur.
Authors:
A Rompel; R M Cinco; M J Latimer; A E McDermott; R D Guiles; A Quintanilha; R M Krauss; K Sauer; V K Yachandra; M P Klein
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  95     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1998 May 
Date Detail:
Created Date:  1998-06-22     Completed Date:  1998-06-22     Revised Date:  2013-06-11    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  6122-7     Citation Subset:  IM    
Affiliation:
Physical Biosciences Division, University of California, Berkeley, CA 94720, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Erythrocytes / metabolism*
Humans
Oxidation-Reduction
Plasma / metabolism*
Spectrometry, X-Ray Emission / methods*
Sulfur
Chemical
Reg. No./Substance:
7704-34-9/Sulfur
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Huntingtin aggregation monitored by dynamic light scattering.
Next Document:  The nature of the excited state of the reaction center of photosystem II of green plants: a high-res...