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Structure, Function, and Mechanism of the Nickel Metalloenzymes, CO Dehydrogenase, and Acetyl-CoA Synthase

Chemical reviews, 2014-04, Vol.114 (8), p.4149-4174

2014

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The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes

Annual review of biochemistry, 2003, Vol.72, p.209-247

2003

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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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Evidence That the Heme Regulatory Motifs in Heme Oxygenase-2 Serve as a Thiol/Disulfide Redox Switch Regulating Heme Binding

The Journal of biological chemistry, 2007-07, Vol.282 (29), p.21056-21067

2007

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Not a “they” but a “we”: The microbiome helps promote our well-being

The Journal of biological chemistry, 2022-02, Vol.298 (2), p.101511-101511, Article 101511

Ragsdale, Stephen W.

2022

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Modulation of nuclear receptor function by cellular redox poise

Journal of inorganic biochemistry, 2014-04, Vol.133, p.92-103

2014

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Heme Regulatory Motifs in Heme Oxygenase-2 Form a Thiol/Disulfide Redox Switch That Responds to the Cellular Redox State

The Journal of biological chemistry, 2009-07, Vol.284 (31), p.20556-20561

2009

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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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High Affinity Heme Binding to a Heme Regulatory Motif on the Nuclear Receptor Rev-erbβ Leads to Its Degradation and Indirectly Regulates Its Interaction with Nuclear Receptor Corepressor

The Journal of biological chemistry, 2016-01, Vol.291 (5), p.2196-2222

2016

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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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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

2018

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Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2

The Journal of biological chemistry, 2007-12, Vol.282 (52), p.37624-37631

2007

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Identification of a Thiol/Disulfide Redox Switch in the Human BK Channel That Controls Its Affinity for Heme and CO

The Journal of biological chemistry, 2010-06, Vol.285 (26), p.20117-20127

2010

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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

2022

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Biochemistry of methyl-coenzyme M reductase: the nickel metalloenzyme that catalyzes the final step in synthesis and the first step in anaerobic oxidation of the greenhouse gas methane

Metal ions in life sciences, 2014-01, Vol.14, p.125

Ragsdale, Stephen W

2014

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Redox, haem and CO in enzymatic catalysis and regulation

Biochemical Society transactions, 2012-06, Vol.40 (3), p.501

2012

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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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Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase

The Journal of biological chemistry, 2014-10, Vol.289 (43), p.29836-29858

2014

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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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Investigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon monoxide dehydrogenases

Metal ions in life sciences, 2014-01, Vol.14, p.71

2014

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Catalysis of methyl group transfers involving tetrahydrofolate and B(12)

Vitamins and hormones, 2008, Vol.79, p.293

Ragsdale, Stephen W

2008

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Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}

The Journal of biological chemistry, 2011-02, Vol.286 (6), p.4392

2011

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Novel and viable acetylcholinesterase target site for developing effective and environmentally safe insecticides

Current drug targets, 2012-04, Vol.13 (4), p.471

2012

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Structure, Function, and Mechanism of the Nickel Metalloenzymes, CO Dehydrogenase, and Acetyl-CoA Synthase

The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes

An unlikely heme chaperone confirmed at last

Evidence That the Heme Regulatory Motifs in Heme Oxygenase-2 Serve as a Thiol/Disulfide Redox Switch Regulating Heme Binding

Not a “they” but a “we”: The microbiome helps promote our well-being

Modulation of nuclear receptor function by cellular redox poise

Heme Regulatory Motifs in Heme Oxygenase-2 Form a Thiol/Disulfide Redox Switch That Responds to the Cellular Redox State

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

High Affinity Heme Binding to a Heme Regulatory Motif on the Nuclear Receptor Rev-erbβ Leads to Its Degradation and Indirectly Regulates Its Interaction with Nuclear Receptor Corepressor

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

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

Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2

Identification of a Thiol/Disulfide Redox Switch in the Human BK Channel That Controls Its Affinity for Heme and CO

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

Biochemistry of methyl-coenzyme M reductase: the nickel metalloenzyme that catalyzes the final step in synthesis and the first step in anaerobic oxidation of the greenhouse gas methane

Redox, haem and CO in enzymatic catalysis and regulation

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

Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase

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

Investigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon monoxide dehydrogenases

Catalysis of methyl group transfers involving tetrahydrofolate and B(12)

Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}

Novel and viable acetylcholinesterase target site for developing effective and environmentally safe insecticides

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