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Characterization of the [2Fe-2S] Cluster of Escherichia coli Transcription Factor IscR

Biochemistry (Easton), 2012-06, Vol.51 (22), p.4453-4462

2012

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Regulation of protein function and degradation by heme, heme responsive motifs, and CO

Critical reviews in biochemistry and molecular biology, 2022-01, Vol.57 (1), p.16-47

2022

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Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site

The Journal of biological chemistry, 2020-12, Vol.295 (50), p.17227-17240

2020

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Spectroscopic and Computational Characterization of the Base-off Forms of Cob(II)alamin

The journal of physical chemistry. B, 2009-04, Vol.113 (15), p.5245-5254

2009

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Redox Regulation of Heme Oxygenase-2 and the Transcription Factor, Rev-Erb, Through Heme Regulatory Motifs

Antioxidants & redox signaling, 2018-12, Vol.29 (18), p.1841-1857

2018

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Iron-containing transcription factors and their roles as sensors

Current opinion in chemical biology, 2011-04, Vol.15 (2), p.335-341

2011

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An unlikely heme chaperone confirmed at last

The Journal of biological chemistry, 2018-09, Vol.293 (37), p.14569-14570

2018

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Regulation of iron–sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe–2S]–IscR in Escherichia coli

Molecular microbiology, 2013-02, Vol.87 (3), p.478-492

2013

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Heme delivery to heme oxygenase-2 involves glyceraldehyde-3-phosphate dehydrogenase

Biological chemistry, 2022-11, Vol.403 (11-12), p.1043-1053

2022

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Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells

The Journal of biological chemistry, 2022-02, Vol.298 (2), p.101549, Article 101549

2022

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Dynamic and structural differences between heme oxygenase-1 and -2 are due to differences in their C-terminal regions

The Journal of biological chemistry, 2019-05, Vol.294 (20), p.8259-8272

2019

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The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation

The Journal of biological chemistry, 2020-04, Vol.295 (16), p.5177-5191

2020

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The C‑Terminal Heme Regulatory Motifs of Heme Oxygenase‑2 Are Redox-Regulated Heme Binding Sites

Biochemistry (Easton), 2015-05, Vol.54 (17), p.2709-2718

2015

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Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases‑1 and -2: Kinetic and Cryoreduction Studies

Biochemistry (Easton), 2016-01, Vol.55 (1), p.62-68

2016

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Spectroscopic Studies Reveal That the Heme Regulatory Motifs of Heme Oxygenase‑2 Are Dynamically Disordered and Exhibit Redox-Dependent Interaction with Heme

Biochemistry (Easton), 2015-05, Vol.54 (17), p.2693-2708

2015

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Ligand Trans Influence Governs Conformation in Cobalamin-Dependent Methionine Synthase

Biochemistry (Easton), 2007-10, Vol.46 (43), p.12382-12392

2007

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Probing the Role of the Histidine 759 Ligand in Cobalamin-Dependent Methionine Synthase

Biochemistry (Easton), 2007-07, Vol.46 (27), p.8024-8035

2007

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Does Activation of the Anti Proton, Rather than Concertedness, Determine the Stereochemistry of Base-Catalyzed 1,2-Elimination Reactions? Anti Stereospecificity in E1cB Eliminations of β-3-Trifluoromethylphenoxy Esters, Thioesters, and Ketones

Journal of organic chemistry, 2012-03, Vol.77 (6), p.2819-2828

2012

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Conversion of Aquifex aeolicus 3-Deoxy-d-manno-octulosonate 8-Phosphate Synthase, a Metalloenzyme, into a Nonmetalloenzyme

Journal of the American Chemical Society, 2004-06, Vol.126 (24), p.7448-7449

2004

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Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site

The Journal of biological chemistry, 2020-12, Vol.295 (50), p.17227

2020

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Spectroscopic Studies Reveal That the Heme Regulatory Motifs of Heme Oxygenase-2 Are Dynamically Disordered and Exhibit Redox-Dependent Interaction with Heme

Biochemistry (Easton), 2015-05, Vol.54 (17)

2015

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The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation

The Journal of biological chemistry, 2020-04, Vol.295 (16), p.5177

2020

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Regulation of iron–sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2 Fe –2 S ]– IscR in E scherichia coli

Molecular microbiology, 2013-02, Vol.87 (3), p.478-492

2013

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Probing the Role of the His759 Ligand in Cobalamin-Dependent Methionine Synthase

Biochemistry (Easton), 2007-06, Vol.46 (27), p.8024-8035

2007

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Implementation of a multilevel, multicomponent intervention for obesity control in Native American communities (OPREVENT2): challenges and lessons learned

Health education research, 2020-06, Vol.35 (3), p.228-242

2020

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Characterization of the [2Fe-2S] Cluster of Escherichia coli Transcription Factor IscR

Regulation of protein function and degradation by heme, heme responsive motifs, and CO

Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site

Spectroscopic and Computational Characterization of the Base-off Forms of Cob(II)alamin

Redox Regulation of Heme Oxygenase-2 and the Transcription Factor, Rev-Erb, Through Heme Regulatory Motifs

Iron-containing transcription factors and their roles as sensors

An unlikely heme chaperone confirmed at last

Regulation of iron–sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2Fe–2S]–IscR in Escherichia coli

Heme delivery to heme oxygenase-2 involves glyceraldehyde-3-phosphate dehydrogenase

Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells

Dynamic and structural differences between heme oxygenase-1 and -2 are due to differences in their C-terminal regions

The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation

The C‑Terminal Heme Regulatory Motifs of Heme Oxygenase‑2 Are Redox-Regulated Heme Binding Sites

Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases‑1 and -2: Kinetic and Cryoreduction Studies

Spectroscopic Studies Reveal That the Heme Regulatory Motifs of Heme Oxygenase‑2 Are Dynamically Disordered and Exhibit Redox-Dependent Interaction with Heme

Ligand Trans Influence Governs Conformation in Cobalamin-Dependent Methionine Synthase

Probing the Role of the Histidine 759 Ligand in Cobalamin-Dependent Methionine Synthase

Does Activation of the Anti Proton, Rather than Concertedness, Determine the Stereochemistry of Base-Catalyzed 1,2-Elimination Reactions? Anti Stereospecificity in E1cB Eliminations of β-3-Trifluoromethylphenoxy Esters, Thioesters, and Ketones

Conversion of Aquifex aeolicus 3-Deoxy-d-manno-octulosonate 8-Phosphate Synthase, a Metalloenzyme, into a Nonmetalloenzyme

Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site

Spectroscopic Studies Reveal That the Heme Regulatory Motifs of Heme Oxygenase-2 Are Dynamically Disordered and Exhibit Redox-Dependent Interaction with Heme

The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation

Regulation of iron–sulphur cluster homeostasis through transcriptional control of the Isc pathway by [2 Fe –2 S ]– IscR in E scherichia coli

Probing the Role of the His759 Ligand in Cobalamin-Dependent Methionine Synthase

Implementation of a multilevel, multicomponent intervention for obesity control in Native American communities (OPREVENT2): challenges and lessons learned

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