Related ArticlesA solution (17)O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase.
Chem Commun (Camb). 2013 Jan 22;49(14):1449-51
Authors: Hanashima S, Fujiwara N, Matsumoto K, Iwasaki N, Zheng GQ, Torigoe H, Suzuki K, Taniguchi N, Yamaguchi Y
Abstract
Solution (17)O-NMR application to biological macromolecules is extremely limited. We describe here (17)O-NMR observation of the (17)O(2)-oxidized cysteine side chain of human Cu,Zn-superoxide dismutase in solution using selective (17)O(2) oxidation. (17)O-NMR with the aid of (17)O-labeling has wide potential to probe the environment and dynamics of oxidizable functionalities in proteins.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
NMR Characterization of a "Fibril-Ready" State of Demetalated Wild-Type Superoxide Dismutase.
J Am Chem Soc. 2010 Dec 16;
Authors: Banci L, Bertini I, Blaževitš O, Cantini F, Lelli M, Luchinat C, Mao J, Vieru M
Demetalated superoxide dismutase (SOD1) is a transient species, fibrillogenic in nature and of biomedical interest. It is a conformationally disordered protein difficult to characterize. We have developed a strategy based on the NMR investigation...
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NMR Characterization of a “Fibril-Ready” State of Demetalated Wild-Type Superoxide Dismutase
NMR Characterization of a “Fibril-Ready” State of Demetalated Wild-Type Superoxide Dismutase
Lucia Banci, Ivano Bertini, Olga Blaževitš, Francesca Cantini, Moreno Lelli, Claudio Luchinat, Jiafei Mao and Miguela Vieru
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1069689/aop/images/medium/ja-2010-069689_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1069689
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[NMR paper] Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected
Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.
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Biochemistry. 2003 Feb 25;42(7):1890-9
Authors: Shipp EL, Cantini F, Bertini I, Valentine JS, Banci L
The backbone assignment of the copper-zinc superoxide dismutase...
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Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-St
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1010305/aop/images/medium/bi-2010-010305_0006.gif
Biochemistry
DOI: 10.1021/bi1010305
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[NMR paper] 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuro
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Authors: Assfalg M, Banci L, Bertini I, Bruschi M, Turano P
The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein,...
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[NMR paper] NMR characterization and solution structure determination of the oxidized cytochrome
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans.
Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14396-400
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A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the...
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J Inorg Biochem. 1990 Jun;39(2):149-59
Authors: Banci L, Bertini I, Caliceti P, MonsĂą Scolaro L, Schiavon O, Veronese FM
Spectroscopic methods have been employed in order to understand the molecular basis of the decrease in enzymatic activity of the antiinflammatory enzyme...
A solution (17)O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase.
Linear Mode
