Search results for: Frank Rusnak

Items from 1 to 20 out of 25 results

article

Purification and characterization of Mycobacterium tuberculosis KatG, KatG(S315T), and Mycobacterium bovis KatG(R463L)

Nancy L. Wengenack, Brian D. Lane, Preston J. Hill, James R. Uhl, more

Protein Expression and Purification > 2004 > 36 > 2 > 232-243

Isoniazid, a first-line antibiotic used for the treatment of tuberculosis, is a prodrug that requires activation by the Mycobacterium tuberculosis enzyme KatG. The KatG(S315T) mutation causes isoniazid resistance while the KatG(R463L) variation is thought to be a polymorphism. Much of the work to date focused on isoniazid activation by KatG has utilized recombinant enzyme overexpressed in Escherichia...

article

Electrochemical Studies of the Mono-Fe, Fe−Zn, and Fe−Fe Metalloisoforms of Bacteriophage λ Protein Phosphatase ^†

Tiffany A. Reiter, Frank Rusnak

Biochemistry > 2004 > 43 > 3 > 782 - 790

article

Formation of a Stable Cyano-Bridged Dinuclear Iron Cluster Following Oxidation of the Superoxide Reductases from Treponema p allidum and Desulfovibrio v ulgaris with K ₃ Fe(CN) ₆ ^‡

Françoise Auchère, Patrícia Raleiras, Linda Benson, Sergei Yu. Venyaminov, more

Inorganic Chemistry > 2003 > 42 > 4 > 938 - 940

article

Mn ²⁺ Is a Native Metal Ion Activator for Bacteriophage λ Protein Phosphatase ^†

Tiffany A. Reiter, Nicholas J. Reiter, Frank Rusnak

Biochemistry > 2002 > 41 > 51 > 15404 - 15409

article

What is the ultimate fate of superoxide anion in vivo?

Franoise Auchre, Frank Rusnak

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 6

Abstract. For three decades, oxidative stress and the role of reactive oxygen species in biology have been extensively studied. Recently, a new interest in these areas has emerged with the discovery of superoxide reductases, a family of familiar bacterial metalloenzymes whose heretofore unknown function has now been apparently revealed. In a series of experiments utilizing genetic, molecular biological,...

article

Is calcineurin a peroxide-specific sensor in T-lymphocytes?

Tiffany Reiter, Frank Rusnak

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 7-8 > 823-834

Abstract. Calcineurin activity in T-lymphocytes has been shown to be sensitive to H2O2. In this report, we investigate the effects of H2O2 and other physiological oxidants on calcineurin activity both in vivo and in vitro. Intracellular calcineurin activity, as determined by NF-AT phosphorylation state and activity, is inhibited by H2O2 but is insensitive to superoxide and NaOCl. Similarly, treatment...

article

Inhibition of Bacteriophage λ Protein Phosphatase by Organic and Oxoanion Inhibitors ^†

Nicholas J. Reiter, Daniel J. White, Frank Rusnak

Biochemistry > 2002 > 41 > 3 > 1051 - 1059

article

The journey from curiosity to function: the mosaic of superoxide reductase is revealed

Frank Rusnak

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 6 > 646-646

article

What is the ultimate fate of superoxide anion in vivo?

Françoise Auchère, Frank Rusnak

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 6 > 664-667

. For three decades, oxidative stress and the role of reactive oxygen species in biology have been extensively studied. Recently, a new interest in these areas has emerged with the discovery of superoxide reductases, a family of familiar bacterial metalloenzymes whose heretofore unknown function has now been apparently revealed. In a series of experiments utilizing genetic, molecular biological,...

article

Evidence for Isoniazid-Dependent Free Radical Generation Catalyzed by Mycobacterium tuberculosi s KatG and the Isoniazid-Resistant Mutant KatG(S315T)

Nancy L. Wengenack, Frank Rusnak

Biochemistry > 2001 > 40 > 30 > 8990 - 8996

article

Identification of the High Affinity Mn ²⁺ Binding Site of Bacteriophage λ Phosphoprotein Phosphatase: Effects of Metal Ligand Mutations on Electron Paramagnetic Resonance Spectra and Phosphatase Activities ^†

Daniel J. White, Nicholas J. Reiter, Robert A. Sikkink, Lian Yu, more

Biochemistry > 2001 > 40 > 30 > 8918 - 8929

article

Carbon Monoxide Adducts of KatG and KatG(S315T) as Probes of the Heme Site and Isoniazid Binding ^†

Gudrun S. Lukat-Rodgers, Nancy L. Wengenack, Frank Rusnak, Kenton R. Rodgers

Biochemistry > 2001 > 40 > 24 > 7149 - 7157

article

Sensing electrons: protein phosphatase redox regulation

Frank Rusnak, Tiffany Reiter

Trends in Biochemical Sciences > 2000 > 25 > 11 > 527-529

article

Desulfoferrodoxin: a modular protein

Carla Ascenso, Frank Rusnak, Ins Cabrito, Maria J. Lima, more

JBIC Journal of Biological Inorganic Chemistry > 2000 > 5 > 6

Abstract. The gene encoding the non-heme iron-containing desulfoferrodoxin from Desulfovibrio vulgaris was cloned in two fragments in order to obtain polypeptides corresponding to the N- and C-terminal domains observed in the tertiary structure. These fragments were expressed in Escherichia coli, purified to homogeneity and biochemically and spectroscopically characterized. Both recombinant fragments...

article

Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia

Jiri Adamec, Frank Rusnak, Whyte G. Owen, Stephen Naylor, more

The American Journal of Human Genetics > 2000 > 67 > 3 > 549-562

Frataxin deficiency is the primary cause of Friedreich ataxia (FRDA), an autosomal recessive cardiodegenerative and neurodegenerative disease. Frataxin is a nuclear-encoded mitochondrial protein that is widely conserved among eukaryotes. Genetic inactivation of the yeast frataxin homologue (Yfh1p) results in mitochondrial iron accumulation and hypersensitivity to oxidative stress. Increased iron deposition...

article

Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774

Jorge Rebelo, Sofia Macieira, João M. Dias, Robert Huber, more

Journal of Molecular Biology > 2000 > 297 > 1 > 135-146

The aldehyde oxidoreductase (MOD) isolated from the sulfate reducer Desulfovibrio desulfuricans (ATCC 27774) is a member of the xanthine oxidase family of molybdenum-containing enzymes. It has substrate specificity similar to that of the homologous enzyme from Desulfovibrio gigas (MOP) and the primary sequences from both enzymes show 68 % identity. The enzyme was crystallized in space group P6 ...

article

Desulfoferrodoxin: a modular protein

Carla Ascenso, Frank Rusnak, Inês Cabrito, Maria J. Lima, more

JBIC Journal of Biological Inorganic Chemistry > 2000 > 5 > 6 > 720-729

. The gene encoding the non-heme iron-containing desulfoferrodoxin from Desulfovibrio vulgaris was cloned in two fragments in order to obtain polypeptides corresponding to the N- and C-terminal domains observed in the tertiary structure. These fragments were expressed in Escherichia coli, purified to homogeneity and biochemically and spectroscopically characterized. Both recombinant fragments behaved...

article

Biochemical and Spectroscopic Characterization of Overexpressed Fuscoredoxin from Escherichia coli

Alice S. Pereira, Pedro Tavares, Carsten Krebs, Boi Hanh Huynh, more

Biochemical and Biophysical Research Communications > 1999 > 260 > 1 > 209-215

Fuscoredoxin is a unique iron containing protein of yet unknown function originally discovered in the sulfate reducers of the genus Desulfovibrio. It contains two iron-sulfur clusters: a cubane [4Fe-4S] and a mixed oxo- and sulfido-bridged 4Fe cluster of unprecedented structure. The recent determination of the genomic sequence of Escherichia coli (E. coli) has revealed a homologue of fuscoredoxin...

article

Mycobacterium tuberculosisKatG Is a Peroxynitritase

Nancy L. Wengenack, Michael P. Jensen, Frank Rusnak, Michael K. Stern

Biochemical and Biophysical Research Communications > 1999 > 256 > 3 > 485-487

Mycobacterium tuberculosisresides within the highly oxidative environment of the human macrophage and previous reports have indicated that these mycobacteria are susceptible to reactive nitrogen intermediates including peroxynitrite. This work provides evidence that theMycobacterium tuberculosishemoprotein KatG acts as an efficient peroxynitritase exhibiting ak _a _p _p of 1.4 x 10 ...

article

Conversion of Desulforedoxin into a Rubredoxin Center

Lian Yu, Matthew Kennedy, Christopher Czaja, Pedro Tavares, more

Biochemical and Biophysical Research Communications > 1997 > 231 > 3 > 679-682

Rubredoxin and desulforedoxin both contain an Fe(S-Cys)₄center. However the spectroscopic properties of the center in desulforedoxin differ from rubredoxin. These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between...

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Search results for: Frank Rusnak

Purification and characterization of Mycobacterium tuberculosis KatG, KatG(S315T), and Mycobacterium bovis KatG(R463L)

Electrochemical Studies of the Mono-Fe, Fe−Zn, and Fe−Fe Metalloisoforms of Bacteriophage λ Protein Phosphatase ^†

Formation of a Stable Cyano-Bridged Dinuclear Iron Cluster Following Oxidation of the Superoxide Reductases from Treponema p allidum and Desulfovibrio v ulgaris with K ₃ Fe(CN) ₆ ^‡

Mn ²⁺ Is a Native Metal Ion Activator for Bacteriophage λ Protein Phosphatase ^†

What is the ultimate fate of superoxide anion in vivo?

Is calcineurin a peroxide-specific sensor in T-lymphocytes?

Inhibition of Bacteriophage λ Protein Phosphatase by Organic and Oxoanion Inhibitors ^†

The journey from curiosity to function: the mosaic of superoxide reductase is revealed

What is the ultimate fate of superoxide anion in vivo?

Evidence for Isoniazid-Dependent Free Radical Generation Catalyzed by Mycobacterium tuberculosi s KatG and the Isoniazid-Resistant Mutant KatG(S315T)

Identification of the High Affinity Mn ²⁺ Binding Site of Bacteriophage λ Phosphoprotein Phosphatase: Effects of Metal Ligand Mutations on Electron Paramagnetic Resonance Spectra and Phosphatase Activities ^†

Carbon Monoxide Adducts of KatG and KatG(S315T) as Probes of the Heme Site and Isoniazid Binding ^†

Sensing electrons: protein phosphatase redox regulation

Desulfoferrodoxin: a modular protein

Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia

Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774

Desulfoferrodoxin: a modular protein

Biochemical and Spectroscopic Characterization of Overexpressed Fuscoredoxin from Escherichia coli

Mycobacterium tuberculosisKatG Is a Peroxynitritase

Conversion of Desulforedoxin into a Rubredoxin Center

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