Crystal structure of Trypanosoma cruzi heme peroxidase and characterization of its substrate specificity and compound I intermediate

[1]  R. Radi,et al.  Cytosolic Fe-superoxide dismutase safeguards Trypanosoma cruzi from macrophage-derived superoxide radical , 2019, Proceedings of the National Academy of Sciences.

[2]  M. Trujillo,et al.  Reactive species and pathogen antioxidant networks during phagocytosis , 2019, The Journal of experimental medicine.

[3]  R. Radi,et al.  Cardiomyocyte diffusible redox mediators control Trypanosoma cruzi infection: role of parasite mitochondrial iron superoxide dismutase. , 2018, The Biochemical journal.

[4]  P. Moody,et al.  The Nature and Reactivity of Ferryl Heme in Compounds I and II. , 2018, Accounts of chemical research.

[5]  Jiahui Chen,et al.  Improvements to the APBS biomolecular solvation software suite , 2017, Protein science : a publication of the Protein Society.

[6]  D. Estrin,et al.  Kinetics, subcellular localization, and contribution to parasite virulence of a Trypanosoma cruzi hybrid type A heme peroxidase (TcAPx-CcP) , 2017, Proceedings of the National Academy of Sciences.

[7]  P. Moody,et al.  Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme , 2016, Nature Communications.

[8]  C. Simmerling,et al.  ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB. , 2015, Journal of chemical theory and computation.

[9]  P. Moody,et al.  Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase , 2014, Science.

[10]  K. M. Bonney,et al.  Chagas disease in the 21st Century: a public health success or an emerging threat? , 2014, Parasite.

[11]  R. Radi,et al.  Trypanosoma cruzi antioxidant enzymes as virulence factors in Chagas disease. , 2013, Antioxidants & redox signaling.

[12]  T. Poulos,et al.  Crystal structure of the Leishmania major peroxidase–cytochrome c complex , 2012, Proceedings of the National Academy of Sciences.

[13]  Emma L Raven,et al.  Crystal structure of guaiacol and phenol bound to a heme peroxidase , 2012, The FEBS journal.

[14]  T. Poulos,et al.  Leishmania major peroxidase is a cytochrome c peroxidase. , 2012, Biochemistry.

[15]  M. Martí,et al.  Molecular basis for the substrate stereoselectivity in tryptophan dioxygenase. , 2011, Biochemistry.

[16]  S. Montgomery,et al.  Trypanosoma cruzi and Chagas' Disease in the United States , 2011, Clinical Microbiology Reviews.

[17]  V. Denysenkov,et al.  Multifrequency electron paramagnetic resonance characterization of PpoA, a CYP450 fusion protein that catalyzes fatty acid dioxygenation. , 2011, Journal of the American Chemical Society.

[18]  T. Poulos,et al.  Crystal Structure of Leishmania major Peroxidase and Characterization of the Compound I Tryptophan Radical* , 2011, The Journal of Biological Chemistry.

[19]  M. N. Álvarez,et al.  Intraphagosomal Peroxynitrite as a Macrophage-derived Cytotoxin against Internalized Trypanosoma cruzi , 2010, The Journal of Biological Chemistry.

[20]  Eileen Kraemer,et al.  TriTrypDB: a functional genomic resource for the Trypanosomatidae , 2009, Nucleic Acids Res..

[21]  P. Moody,et al.  Engineering the substrate specificity and reactivity of a heme protein: creation of an ascorbate binding site in cytochrome c peroxidase. , 2008, Biochemistry.

[22]  A. Ivancich,et al.  Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy. , 2008, Biochemistry.

[23]  J. Erman,et al.  Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: evidence for a single, catalytically active, cytochrome c binding domain. , 2008, Biochemistry.

[24]  Randy J. Read,et al.  Phaser crystallographic software , 2007, Journal of applied crystallography.

[25]  L. Ghamsari,et al.  Interaction of ascorbate peroxidase with substrates: a mechanistic and structural analysis. , 2006, Biochemistry.

[26]  S. Adak,et al.  Leishmania major encodes an unusual peroxidase that is a close homologue of plant ascorbate peroxidase: a novel role of the transmembrane domain. , 2005, The Biochemical journal.

[27]  D. Horn,et al.  Vitamin C biosynthesis in trypanosomes: a role for the glycosome. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[28]  Fei Long,et al.  REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. , 2004, Acta crystallographica. Section D, Biological crystallography.

[29]  Robert C. Edgar,et al.  MUSCLE: a multiple sequence alignment method with reduced time and space complexity , 2004, BMC Bioinformatics.

[30]  G. Crooks,et al.  WebLogo: a sequence logo generator. , 2004, Genome research.

[31]  G. Jeschke EPR techniques for studying radical enzymes. , 2004, Biochimica et biophysica acta.

[32]  E. Raven Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase? , 2003, Natural product reports.

[33]  M. Mewies,et al.  Crystal structure of the ascorbate peroxidase–ascorbate complex , 2003, Nature Structural Biology.

[34]  M. Mewies,et al.  Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites. , 2002, Biochemistry.

[35]  Samson O Obado,et al.  Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[36]  Jaswir Basran,et al.  Role of histidine 42 in ascorbate peroxidase. Kinetic analysis of the H42A and H42E variants. , 2002, European journal of biochemistry.

[37]  B. Sjöberg,et al.  Protein thiyl radicals directly observed by EPR spectroscopy. , 2002, Archives of biochemistry and biophysics.

[38]  W. Lubitz,et al.  Tryptophan and tyrosine radicals in ribonucleotide reductase: a comparative high-field EPR study at 94 GHz. , 2001, Biochemistry.

[39]  D. Goodin,et al.  Multifrequency high-field EPR study of the tryptophanyl and tyrosyl radical intermediates in wild-type and the W191G mutant of cytochrome c peroxidase. , 2001, Journal of the American Chemical Society.

[40]  B. Hoffman,et al.  Cytochrome c peroxidase-cytochrome c complex: locating the second binding domain on cytochrome c peroxidase with site-directed mutagenesis. , 2000, Biochemistry.

[41]  T. Poulos,et al.  Conversion of an Engineered Potassium-binding Site into a Calcium-selective Site in Cytochrome c Peroxidase* , 1999, The Journal of Biological Chemistry.

[42]  T. Poulos,et al.  The effects of an engineered cation site on the structure, activity, and EPR properties of cytochrome c peroxidase. , 1999, Biochemistry.

[43]  J. Dawson,et al.  Spectroscopic study of the compound ES and the oxoferryl compound II states of cytochrome c peroxidase: comparison with the compound II of horseradish peroxidase , 1998 .

[44]  T. Poulos,et al.  An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan. , 1996, Biochemistry.

[45]  J. B. Park,et al.  Vitamin C pharmacokinetics in healthy volunteers: evidence for a recommended dietary allowance. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[46]  T. Poulos,et al.  Identification of a porphyrin pi cation radical in ascorbate peroxidase compound I. , 1995, Biochemistry.

[47]  M. Albrecht,et al.  Ascorbate variations and dehydroascorbate reductase activity in Trypanosoma cruzi epimastigotes and trypomastigotes. , 1994, Molecular and biochemical parasitology.

[48]  J. Kraut,et al.  Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. , 1993, Science.

[49]  D. Singel,et al.  High-frequency (139.5 GHz) EPR spectroscopy of the tyrosyl radical in Escherichia coli ribonucleotide reductase , 1993 .

[50]  D B Goodin,et al.  Comprehensive explanation of the anomalous EPR spectra of wild-type and mutant cytochrome c peroxidase compound ES. , 1993, Biochemistry.

[51]  R. Stephens,et al.  Sequence logos: a new way to display consensus sequences. , 1990, Nucleic acids research.

[52]  E. Myers,et al.  Basic local alignment search tool. , 1990, Journal of molecular biology.

[53]  D B Goodin,et al.  Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. , 1989, Science.

[54]  W. L. Jorgensen,et al.  Comparison of simple potential functions for simulating liquid water , 1983 .

[55]  P. Afonine,et al.  research papers Acta Crystallographica Section D Biological , 2003 .

[56]  B. Sjöberg,et al.  Generation and electron paramagnetic resonance spin trapping detection of thiyl radicals in model proteins and in the R1 subunit of Escherichia coli ribonucleotide reductase. , 2002, Archives of biochemistry and biophysics.

[57]  E. Raven Peroxidase-catalyzed oxidation of ascorbate. Structural, spectroscopic and mechanistic correlations in ascorbate peroxidase. , 2000, Sub-cellular biochemistry.

[58]  M. Miles,et al.  Trypanosoma cruzi: zymodemes associated with acute and chronic Chagas' disease in central Brazil. , 1986, Transactions of the Royal Society of Tropical Medicine and Hygiene.

[59]  D P Nelson,et al.  Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H 2 O 2 solutions in the UV). , 1972, Analytical biochemistry.