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Sublethal Paraquat Confers Multidrug Tolerance in Pseudomonas aeruginosa by Inducing Superoxide Dismutase Activity and Lowering Envelope Permeability.

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Stressors and environmental cues shape the physiological state of bacteria, and thus how they subsequently respond to antibiotic toxicity. To understand how superoxide stress can modulate survival to bactericidal antibiotics, we examined the effect of intra...

Article GUID: 33101252

Ctt1 catalase activity potentiates antifungal azoles in the emerging opportunistic pathogen Saccharomyces cerevisiae.

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Sci Rep. 2019 Jun 24;9(1):9185 Authors: Martins D, Nguyen D, English AM

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Derivatization of yeast cytochrome c peroxidase with pentaammineruthenium(III).

Author(s): Fox T, English AM, Gibbs BF

Derivatization of yeast cytochrome c peroxidase with pentaammineruthenium(III).
Bioconjug Chem. 1994 Jan-Feb;5(1):14-20
Authors: Fox T, English AM, Gibbs BF
Abstract
Cytochrome c peroxidase (CCP) was derivatized using aquopentaamminerutheniu...

Article GUID: 8199229

Mass spectral analysis of protein-based radicals using DBNBS. Nonradical adduct formation versus spin trapping.

Author(s): Filosa A, English AM

J Biol Chem. 2001 Jun 15;276(24):21022-7 Authors: Filosa A, English AM

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Heme nitrosylation of deoxyhemoglobin by s-nitrosoglutathione requires copper.

Author(s): Romeo AA, Capobianco JA, English AM

J Biol Chem. 2002 Jul 05;277(27):24135-41 Authors: Romeo AA, Capobianco JA, English AM

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S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain.

Author(s): Tao L, Murphy ME, English AM

Biochemistry. 2002 May 14;41(19):6185-92 Authors: Tao L, Murphy ME, English AM

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Different pathways of radical translocation in yeast cytochrome c peroxidase and its W191F mutant on reaction with H(2)O(2) suggest an antioxidant role.

Author(s): Tsaprailis G, English AM

J Biol Inorg Chem. 2003 Feb;8(3):248-55 Authors: Tsaprailis G, English AM

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Mechanism of S-nitrosation of recombinant human brain calbindin D28K.

Author(s): Tao L, English AM

Biochemistry. 2003 Mar 25;42(11):3326-34 Authors: Tao L, English AM

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Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine.

Author(s): Jiang H, English AM

J Proteome Res. 2002 Jul-Aug;1(4):345-50 Authors: Jiang H, English AM

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Scavenging with TEMPO* to identify peptide- and protein-based radicals by mass spectrometry: advantages of spin scavenging over spin trapping.

Author(s): Wright PJ, English AM

J Am Chem Soc. 2003 Jul 16;125(28):8655-65 Authors: Wright PJ, English AM

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ESI-MS and FTIR studies of the interaction between the second PDZ domain of hPTP1E and target peptides.

Author(s): Papp R, Ekiel I, English AM

Biochem Cell Biol. 2003 Apr;81(2):71-80 Authors: Papp R, Ekiel I, English AM

Article GUID: 12870871

Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein.

Author(s): Romeo AA, Capobianco JA, English AM

J Am Chem Soc. 2003 Nov 26;125(47):14370-8 Authors: Romeo AA, Capobianco JA, English AM

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Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione.

Author(s): Tao L, English AM

Biochemistry. 2004 Apr 06;43(13):4028-38 Authors: Tao L, English AM

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Mass spectrometric analysis of nitroxyl-mediated protein modification: comparison of products formed with free and protein-based cysteines.

Author(s): Shen B, English AM

Biochemistry. 2005 Oct 25;44(42):14030-44 Authors: Shen B, English AM

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Hemoglobin S-nitrosation on oxygenation of nitrite/deoxyhemoglobin incubations is attenuated by methemoglobin.

Author(s): Laterreur J, English AM

J Inorg Biochem. 2007 Nov;101(11-12):1827-35 Authors: Laterreur J, English AM

Article GUID: 17889368

ESI-MS quantitation of iron as its 4-(2-pyridylazo)resorcinol (PAR) complex: application to pharmaceutical tablets containing iron oxide pigment.

Author(s): Susanto D, English AM, Sharma R, Kwong E

J Mass Spectrom. 2011 May;46(5):508-16 Authors: Susanto D, English AM, Sharma R, Kwong E

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SOD1 oxidation and formation of soluble aggregates in yeast: relevance to sporadic ALS development.

Author(s): Martins D, English AM

Redox Biol. 2014;2:632-9 Authors: Martins D, English AM

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Targeted proteomics identify metabolism-dependent interactors of yeast cytochrome c peroxidase: implications in stress response and heme trafficking.

Author(s): Kathiresan M, English AM

Metallomics. 2016 Apr;8(4):434-43 Authors: Kathiresan M, English AM

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LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess H2O2.

Author(s): Kathiresan M, English AM

Chem Sci. 2017 Feb 01;8(2):1152-1162 Authors: Kathiresan M, English AM

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Superoxide dismutase activity confers (p)ppGpp-mediated antibiotic tolerance to stationary-phase Pseudomonas aeruginosa.

Author(s): Martins D, McKay G, Sampathkumar G, Khakimova M, English AM, Nguyen D

Proc Natl Acad Sci U S A. 2018 09 25;115(39):9797-9802 Authors: Martins D, McKay G, Sampathkumar G, Khakimova M, English AM, Nguyen D

Article GUID: 30201715


Title:Derivatization of yeast cytochrome c peroxidase with pentaammineruthenium(III).
Authors:Fox TEnglish AMGibbs BF
Link:www.ncbi.nlm.nih.gov/pubmed/8199229?dopt=Abstract
DOI:10.1021/bc00025a003
Category:Bioconjug Chem
PMID:8199229
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, Montreal, Québec, Canada.

Description:

Derivatization of yeast cytochrome c peroxidase with pentaammineruthenium(III).

Bioconjug Chem. 1994 Jan-Feb;5(1):14-20

Authors: Fox T, English AM, Gibbs BF

Abstract

Cytochrome c peroxidase (CCP) was derivatized using aquopentaammineruthenium(II) [a5RuIIH2O] resulting in stable, covalently-linked derivatives that were purified by cation-exchange FPLC. Spectrophotometric determination of a5RuHis:heme ratios allowed identification of two derivatives containing one a5RuHis per CCP molecule. The histidine-specific reagent, diethyl pyrocarbonate (DEPC), which reacted with three histidine residues in native CCP (6, 60, 96) at pH 7, reacted with only two histidines in both a5RuHisCCP species. X-ray crystallography showed that a5Ru is coordinated to His60 in one derivative [Fox et al. (1990) J. Am. Chem. Soc. 112, 7426]; HPLC and mass spectral analysis of the tryptic peptides of the other derivative identified a peptide (MW = 1469 Da) corresponding to residues 1-12 of CCP plus a5Ru, indicating His6 as the site of modification. Mass spectral analysis of native CCP, a5RuHis60CCP, and the a5RuHis6 derivative yielded MWs of 33,536, 33,717, and 33,901 Da, respectively, revealing that a second site is ruthenated in the His6 derivative. Mass spectral analysis of a shoulder separated from the a5RuHis60CCP FPLC peak also indicated the presence of CCP with bound a5Ru (MW = 33,718 Da). Differential pulse voltammetry of this shoulder, which has negligible a5RuHis absorption, gave a peak at -68 mV (vs NHE) which is in the range expected for reduction of a5RuIII (carboxylato) complexes, as well as a peak at 42 mV due to the presence of approximately 20% a5RuHis60CCP. The extent of ruthenation at sites other than histidine was unexpected and illustrates that a5RuIIH2O is less specific for histidine than previously thought. Activity measurements and stability of enzyme intermediates were measured to further characterize the a5RuCCP species and showed that the derivatives have similar properties to native CCP.

PMID: 8199229 [PubMed - indexed for MEDLINE]