Gudrun S. Lukat-Rodgers

article

Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae

Rizvan C. Uluisik, Neval Akbas, Gudrun S. Lukat-Rodgers, Seth A. Adrian, more

Journal of Inorganic Biochemistry > 2017 > 167 > C > 124-133

HtaA is a heme-binding protein that is part of the heme uptake system in Corynebacterium diphtheriae. HtaA contains two conserved regions (CR1 and CR2). It has been previously reported that both domains can bind heme; the CR2 domain binds hemoglobin more strongly than the CR1 domain. In this study, we report the biophysical characteristics of HtaA-CR2. UV–visible spectroscopy and resonance Raman experiments...

article

CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

Judy P. Hines, Aaron T. Smith, Jose P. Jacob, Gudrun S. Lukat-Rodgers, more

JBIC Journal of Biological Inorganic Chemistry > 2016 > 21 > 8 > 1021-1035

The RNA-binding heme protein DiGeorge critical region 8 (DGCR8) and its ribonuclease partner Drosha cleave primary transcripts of microRNA (pri-miRNA) as part of the canonical microRNA (miRNA) processing pathway. Previous studies show that bis-cysteine thiolate-coordinated Fe(III) DGCR8 supports pri-miRNA processing activity, while Fe(II) DGCR8 does not. In this study, we further characterized Fe(II)...

article

Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization

Elizabeth B. Draganova, Seth A. Adrian, Gudrun S. Lukat-Rodgers, Cyrianne S. Keutcha, more

JBIC Journal of Biological Inorganic Chemistry > 2016 > 21 > 7 > 875-886

The heme-binding protein HmuT is part of the Corynebacterium diphtheriae heme uptake pathway and is responsible for the delivery of heme to the HmuUV ABC transporter. HmuT binds heme with a conserved His/Tyr heme axial ligation motif. Sequence alignment revealed additional conserved residues of potential importance for heme binding: R237, Y272 and M292. In this study, site-directed mutations at these...

article

Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor

David Z. Mokry, Angela Nadia-Albete, Michael K. Johnson, Gudrun S. Lukat-Rodgers, more

BBA - General Subjects > 2014 > 1840 > 10 > 3058-3066

For many pathogenic microorganisms, iron acquisition represents a significant stress during the colonization of a mammalian host. Heme is the single most abundant source of soluble iron in this environment. While the importance of iron assimilation for nearly all organisms is clear, the mechanisms by which heme is acquired and utilized by many bacterial pathogens, even those most commonly found at...

article

Plasmodium falciparum: Nitric oxide modulates heme speciation in isolated food vacuoles

Graciela Ostera, Fuyuki Tokumasu, Clarissa Teixeira, Nicolas Collin, more

Experimental Parasitology > 2011 > 127 > 1 > 1-8

Nitric oxide (NO) and NO-derived reactive nitrogen species (RNS) are present in the food vacuole (FV) of Plasmodium falciparum trophozoites. The product of PFL1555w, a putative cytochrome b ₅ , localizes in the FV membrane, similar to what was previously observed for the product of PF13_0353, a putative cytochrome b ₅ reductase. These two gene products may contribute to NO generation...

article

Heme-Based Sensing by the Mammalian Circadian Protein CLOCK

Gudrun S. Lukat-Rodgers, Cristina Correia, Maria Victoria Botuyan, Georges Mer, more

Inorganic Chemistry > 2010 > 49 > 14 > 6349 - 6365

article

How Active-Site Protonation State Influences the Reactivity and Ligation of the Heme in Chlorite Dismutase

Bennett R. Streit, Béatrice Blanc, Gudrun S. Lukat-Rodgers, Kenton R. Rodgers, more

Journal of the American Chemical Society > 2010 > 132 > 16 > 5711 - 5724

article

Role of conserved Fα-helix residues in the native fold and stability of the kinase-inhibited oxy state of the oxygen-sensing FixL protein from Sinorhizobium meliloti

Mark F. Reynolds, Lindsey Ackley, Alice Blizman, Zachary Lutz, more

Archives of Biochemistry and Biophysics > 2009 > 485 > 2 > 150-159

The oxygen-sensing FixL protein from Sinorhizobium meliloti is part of the heme-PAS family of gas sensors that regulate many important signal transduction pathways in a wide variety of organisms. We examined the role of the conserved F _α -9 arginine 200 and several other conserved residues on the proximal F _α -helix in the heme domain of SmFixL* using site-directed mutagenesis in conjunction...

article

Identification of Two Heme-Binding Sites in the Cytoplasmic Heme-Trafficking Protein PhuS from Pseudomonas aeruginosa and Their Relevance to Function ^†

Darci R. Block, Gudrun S. Lukat-Rodgers, Kenton R. Rodgers, Angela Wilks, more

Biochemistry > 2007 > 46 > 50 > 14391 - 14402

article

Insight into Heme Protein Redox Potential Control and Functional Aspects of Six-Coordinate Ligand-Sensing Heme Proteins from Studies of Synthetic Heme Peptides

Aaron B. Cowley, Michelle L. Kennedy, Svetlana Silchenko, Gudrun S. Lukat-Rodgers, more

Inorganic Chemistry > 2006 > 45 > 25 > 9985 - 10001

article

The Heme of Cystathionine β-synthase Likely Undergoes a Thermally Induced Redox-Mediated Ligand Switch ^†

Samuel Pazicni, Melisa M. Cherney, Gudrun S. Lukat-Rodgers, Jana Oliveriusová, more

Biochemistry > 2005 > 44 > 51 > 16785 - 16795

article

Characterization of the Periplasmic Heme-Binding Protein ShuT from the Heme Uptake System of Shigella dysenteriae ^†

Suntara Eakanunkul, Gudrun S. Lukat-Rodgers, Suganya Sumithran, Arundhati Ghosh, more

Biochemistry > 2005 > 44 > 39 > 13179 - 13191

article

Insights into heme-based O2 sensing from structure–function relationships in the FixL proteins

Kenton R. Rodgers, Gudrun S. Lukat-Rodgers

Journal of Inorganic Biochemistry > 2005 > 99 > 4 > 963-977

FixL proteins are bacterial heme-containing signal transduction proteins responsible for sensing the O ₂ concentration in the organism’s environment. In Sinorhizobium meliloti FixL is a protein histidine kinase that, together with its response regulator FixJ, constitute an oxygen-sensitive switch for regulation of the organism’s nitrogen fixation and microaerobic respiration genes. The O ...

article

The Redox Behavior of the Heme in Cystathionine β-synthase Is Sensitive to pH ^†

Samuel Pazicni, Gudrun S. Lukat-Rodgers, Jana Oliveriusová, Katherine A. Rees, more

Biochemistry > 2004 > 43 > 46 > 14684 - 14695

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

A Possible Role for the Covalent Heme−Protein Linkage in Cytochrome c Revealed via Comparison of N -Acetylmicroperoxidase-8 and a Synthetic, Monohistidine-Coordinated Heme Peptide ^†

Aaron B. Cowley, Gudrun S. Lukat-Rodgers, Kenton R. Rodgers, David R. Benson

Biochemistry > 2004 > 43 > 6 > 1656 - 1666

article

Comparison of Thioethers and Sulfoxides as Axial Ligands for N -Acetylmicroperoxidase-8: Implications for Oxidation of Methionine-80 in Cytochrome c

Gerald H. Lushington, Aaron B. Cowley, Svetlana Silchenko, Gudrun S. Lukat-Rodgers, more

Inorganic Chemistry > 2003 > 42 > 23 > 7550 - 7559

article

Insights into the Signal Transduction Mechanism of Rm FixL Provided by Carbon Monoxide Recombination Kinetics ^†

Kenton R. Rodgers, Lei Tang, Gudrun S. Lukat-Rodgers, Nancy L. Wengenack

Biochemistry > 2001 > 40 > 43 > 12932 - 12942

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

Nitrosyl adducts of FixL as probes of heme environment

Kenton R. Rodgers, Gudrun S. Lukat-Rodgers, Lei Tang

JBIC Journal of Biological Inorganic Chemistry > 2000 > 5 > 5 > 642-654

Abstract. This report presents a spectroscopic investigation of the nitrosyl adducts of FixL, the sensor in the signal transduction system responsible for regulating nitrogen fixation in Rhizobium meliloti. Variable-temperature resonance Raman (RR), electron spin resonance (ESR), and variable-temperature UV-visible absorption data are presented for the ferrous NO adducts of two FixL deletion derivatives,...

INFONA - science communication portal

Search results for: Gudrun S. Lukat-Rodgers

Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae

CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization

Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor

Plasmodium falciparum: Nitric oxide modulates heme speciation in isolated food vacuoles

Heme-Based Sensing by the Mammalian Circadian Protein CLOCK

How Active-Site Protonation State Influences the Reactivity and Ligation of the Heme in Chlorite Dismutase

Role of conserved Fα-helix residues in the native fold and stability of the kinase-inhibited oxy state of the oxygen-sensing FixL protein from Sinorhizobium meliloti

Identification of Two Heme-Binding Sites in the Cytoplasmic Heme-Trafficking Protein PhuS from Pseudomonas aeruginosa and Their Relevance to Function ^†

Insight into Heme Protein Redox Potential Control and Functional Aspects of Six-Coordinate Ligand-Sensing Heme Proteins from Studies of Synthetic Heme Peptides

The Heme of Cystathionine β-synthase Likely Undergoes a Thermally Induced Redox-Mediated Ligand Switch ^†

Characterization of the Periplasmic Heme-Binding Protein ShuT from the Heme Uptake System of Shigella dysenteriae ^†

Insights into heme-based O2 sensing from structure–function relationships in the FixL proteins

The Redox Behavior of the Heme in Cystathionine β-synthase Is Sensitive to pH ^†

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

A Possible Role for the Covalent Heme−Protein Linkage in Cytochrome c Revealed via Comparison of N -Acetylmicroperoxidase-8 and a Synthetic, Monohistidine-Coordinated Heme Peptide ^†

Comparison of Thioethers and Sulfoxides as Axial Ligands for N -Acetylmicroperoxidase-8: Implications for Oxidation of Methionine-80 in Cytochrome c

Insights into the Signal Transduction Mechanism of Rm FixL Provided by Carbon Monoxide Recombination Kinetics ^†

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

Nitrosyl adducts of FixL as probes of heme environment

Filter options

Publication date

Keywords

Data set

Journal

INFONA - science communication portal

Search results for: Gudrun S. Lukat-Rodgers

Add recipient

Sending message cancelled

Are you sure you want to cancel sending this message?

Send message

Filter options

Publication date

Date range setting

Set the date range to filter the displayed results. You can set a starting date, ending date or both. You can enter the dates manually or choose them from the calendar.

Keywords

Data set

Journal

Reporting an error / abuse

Sending the report failed

Accessibility options