Using Microwave-Assisted Metal-Catalyzed Oxidation Reactions and Mass Spectrometry To Increase the Rate at Which the Copper-Binding Sites of a Protein Are Determined

2005 ◽  
Vol 77 (14) ◽  
pp. 4649-4653 ◽  
Author(s):  
Juma D. Bridgewater ◽  
Richard W. Vachet
Keyword(s):  
Mass Spectrometry ◽  
Binding Sites ◽  
Copper Binding ◽  
Oxidation Reactions ◽  
Microwave Assisted ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation ◽  
Copper Binding Sites

Transition Metal−Peptide Binding Studied by Metal-Catalyzed Oxidation Reactions and Mass Spectrometry

2006 ◽  
Vol 78 (7) ◽  
pp. 2432-2438 ◽  
Author(s):  
Juma D. Bridgewater ◽  
Jihyeon Lim ◽  
Richard W. Vachet
Keyword(s):  
Mass Spectrometry ◽  
Transition Metal ◽  
Peptide Binding ◽  
Oxidation Reactions ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation

scholarly journals Identification of the Copper(II) Coordinating Residues in the Prion Protein by Metal-Catalyzed Oxidation Mass Spectrometry: Evidence for Multiple Isomers at Low Copper(II) Loadings†

Biochemistry ◽  
2008 ◽  
Vol 47 (35) ◽  
pp. 9258-9268 ◽  
Author(s):  
Rapole Srikanth ◽  
Jonathan Wilson ◽  
Colin S. Burns ◽  
Richard W. Vachet
Keyword(s):  
Mass Spectrometry ◽  
Prion Protein ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation

scholarly journals Metal-catalyzed oxidation of human serum albumin does not alter the interactive binding to the two principal drug binding sites

2018 ◽  
Vol 14 ◽  
pp. 155-160 ◽  
Author(s):  
Keishi Yamasaki ◽  
Koji Nishi ◽  
Makoto Anraku ◽  
Kazuaki Taguchi ◽  
Toru Maruyama ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Drug Binding Sites ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation

scholarly journals Metal-catalyzed oxidation of Aβ and the resulting reorganization of Cu binding sites promote ROS production

Metallomics ◽  
2016 ◽  
Vol 8 (10) ◽  
pp. 1081-1089 ◽  
Author(s):  
Clémence Cheignon ◽  
Peter Faller ◽  
Denis Testemale ◽  
Christelle Hureau ◽  
Fabrice Collin
Keyword(s):  
Binding Sites ◽  
The Self ◽  
Ros Production ◽  
Copper Coordination ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation

Aβ oxidation due to HO˙ production by Cu–Aβ/ascorbate changes copper coordination and leads to the self-enhancement of HO˙ production and release.

scholarly journals Scleroderma Autoantigens Are Uniquely Fragmented by Metal-catalyzed Oxidation Reactions: Implications for Pathogenesis

1997 ◽  
Vol 185 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Livia Casciola-Rosen ◽  
Fredrick Wigley ◽  
Antony Rosen
Keyword(s):  
Reactive Oxygen Species ◽  
Ischemia Reperfusion ◽  
Reactive Oxygen ◽  
Autoimmune Response ◽  
Dependent Manner ◽  
Oxygen Species ◽  
Oxidation Reactions ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation

The observation that revelation of immunocryptic epitopes in self antigens may initiate the autoimmune response has prompted the search for processes which induce novel fragmentation of autoantigens as potential initiators of autoimmunity. The reversible ischemia reperfusion which characterizes scleroderma has focused attention on reactive oxygen species as molecules which might induce autoantigen fragmentation. We demonstrate that several of the autoantigens targeted in diffuse scleroderma are uniquely susceptible to cleavage by reactive oxygen species, in a metal-dependent manner. Multiple features of the fragmentation reaction and its inhibition indicate that these autoantigens possess metal-binding sites, which focus metal-catalyzed oxidation reactions (and consequent fragmentation) to specific regions of the antigens. These data suggest that the autoantibody response in scleroderma is the immune marker of unique protein fragmentation, induced by ischemia reperfusion in the presence of appropriate metals, and focus attention on abnormal metal status as a potential pathogenic principle in this disease.

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