Copper-catalyzed Protein Oxidation and Its Modulation by Carbon Dioxide

Ramirez, Dario C.; Gomez-Mejiba, Sandra E.; Mason, Ronald P.

doi:10.1074/jbc.m504241200

Cited by 71 publications

(81 citation statements)

References 54 publications

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“…For example, the highly reactive carbonate radical anion (CO À 3 ) is thought to form when a complex of peroxide with CO 2 is reduced by a proteinCu(I) complex (Ramirez et al 2005). Similarly, bicarbonate has been shown to enhance peroxide-catalyzed oxidation of proteins as a result of formation of the reactive peroxymonocarbonate ion, HCO À 4 (Richardson et al 2003).…”

Section: Discussionmentioning

confidence: 99%

Increased protein carbonylation in leaves of Arabidopsis and soybean in response to elevated [CO2]

et al. 2008

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While exposure of C 3 plants to elevated [CO 2 ] would be expected to reduce production of reactive oxygen species (ROS) revealed that both treatments altered the abundance of a similar subset of proteins, consistent with the idea that both conditions may involve an oxidative stress. The 2-DE analysis of leaf proteins was facilitated by a novel and simple procedure to remove ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from soluble soybean leaf extracts. Collectively, these findings add a new dimension to our understanding of global change biology and raise the possibility that oxidative signals can be an unexpected component of plant response to elevated [CO 2 ].

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Section: Discussionmentioning

confidence: 99%

Increased protein carbonylation in leaves of Arabidopsis and soybean in response to elevated [CO2]

et al. 2008

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“…A recent crystal structure of PSII-WOC from T. elongutus at 3.5 Å resolution has proposed the atomic structure to consist of an Mn 4 CaO 4 core, having four oxo/hydroxo/aquo ligands bridging the metals to form a cubical Mn 3 CaO 4 subcore that is bridged to the fourth external Mn atom at one of the corner oxos 4 , although this model remains debated 9,10 . The XRD data provides evidence for the presence of a planar ligand in the active site, suggested to be HCO 3 -/CO 3 2-or NO 3 -that is positioned between Ca and the external Mn atom. Site directed mutagenesis of the protein residue that defines the binding site has provided some support for a possible functional bicarbonate at this location.…”

Section: Introductionmentioning

confidence: 98%

Carbonate Complexation of Mn²⁺ in the Aqueous Phase: Redox Behavior and Ligand Binding Modes by Electrochemistry and EPR Spectroscopy

et al. 2006

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The chemical speciation of Mn 2+ within cells is critical for its transport, availability and redox properties. Herein we investigate the redox behavior and complexation equilibria of Mn 2+ in aqueous solutions of bicarbonate by voltametry and electron paramagnetic resonance (EPR) spectroscopy, and discuss the implications for the uptake of Mn 2+ by mangano-cluster enzymes like photosystem II (PSII). Both the electrochemical reduction of Mn 2+ to Mn 0 at an Hg electrode and EPR (in the absence of a polarizing electrode), revealed formation of 1:1 and 1:2 Mn-(bi)carbonate complexes as a function of Mn 2+ and bicarbonate concentrations. Pulsed EPR spectroscopy, including ENDOR, ESEEM and 2D-HYSCORE, were used to probe the hyperfine couplings to 1 H and 13 C nuclei of the ligand(s) bound to Mn 2+ . For the 1:2 complex the complete 13 C hyperfine tensor for one of the (bi) carbonate ligands was determined and it was established that this ligand coordinates to Mn 2+ in bidentate mode with 13 C-Mn distance of 2.85 ± 0.1 Å. The second (bi)carbonate ligand in the 1:2 complex coordinates possibly in monodentate mode, which is structurally less defined, and its 13 C signal is broad and unobservable. 1 H ENDOR reveals that 1-2 water ligands are lost upon binding of one bicarbonate ion in the 1:1 complex while 3-4 water ligands are lost upon forming the 1:2 complex. Thus, we deduce that the dominant species above 0.1 M bicarbonate concentration is the 1:2 complex, [Mn(CO 3 )(HCO 3 )(OH 2 ) 3 ] -.

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“…also toxic to cells and can damage phospholipids, enzymes and nucleic acids (Yoshida et al 1993;Ramirez et al 2005). Therefore uptake, intracellular distribution and export of copper have to be tightly regulated.…”

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confidence: 99%

Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking

et al. 2008

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The CopA copper ATPase of Enterococcus hirae belongs to the family of heavy metal pumping CPx-type ATPases and shares 43% sequence similarity with the human Menkes and Wilson copper ATPases. Due to a lack of suitable protein crystals, only partial three-dimensional structures have so far been obtained for this family of ion pumps. We present a structural model of CopA derived by combining topological information obtained by intramolecular cross-linking with molecular modeling. Purified CopA was crosslinked with different bivalent reagents, followed by tryptic digestion and identification of cross-linked peptides by mass spectrometry. The structural proximity of tryptic fragments provided information about the structural arrangement of the hydrophilic protein domains, which was integrated into a three-dimensional model of CopA. Comparative modeling of CopA was guided by the sequence similarity to the calcium ATPase of the sarcoplasmic reticulum, Serca1, for which detailed structures are available. In addition, known partial structures of CPx-ATPase homologous to CopA were used as modeling templates. A docking approach was used to predict the orientation of the heavy metal binding domain of CopA relative to the core structure, which was verified by distance constraints derived from cross-links. The overall structural model of CopA resembles the Serca1 structure, but reveals distinctive features of CPx-type ATPases. A prominent feature is the positioning of the heavy metal binding domain. It features an orientation of the Cu binding ligands which is appropriate for the interaction with Cu-loaded metallochaperones in solution. Moreover, a novel model of the architecture of the intramembranous Cu binding sites could be derived.

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Copper-catalyzed Protein Oxidation and Its Modulation by Carbon Dioxide

Cited by 71 publications

References 54 publications

Increased protein carbonylation in leaves of Arabidopsis and soybean in response to elevated [CO2]

Increased protein carbonylation in leaves of Arabidopsis and soybean in response to elevated [CO2]

Carbonate Complexation of Mn²⁺ in the Aqueous Phase: Redox Behavior and Ligand Binding Modes by Electrochemistry and EPR Spectroscopy

Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking

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Copper-catalyzed Protein Oxidation and Its Modulation by Carbon Dioxide

Cited by 71 publications

References 54 publications

Increased protein carbonylation in leaves of Arabidopsis and soybean in response to elevated [CO2]

Increased protein carbonylation in leaves of Arabidopsis and soybean in response to elevated [CO2]

Carbonate Complexation of Mn2+ in the Aqueous Phase: Redox Behavior and Ligand Binding Modes by Electrochemistry and EPR Spectroscopy

Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking

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Carbonate Complexation of Mn²⁺ in the Aqueous Phase: Redox Behavior and Ligand Binding Modes by Electrochemistry and EPR Spectroscopy