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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 radical mechanism of biological methane synthesis by methyl-coenzyme M reductase

Science (American Association for the Advancement of Science), 2016-05, Vol.352 (6288), p.953-958

2016

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Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation

Chemical reviews, 2013-08, Vol.113 (8), p.6621-6658

2013

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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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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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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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Thiol/Disulfide redox switches in the regulation of heme binding to proteins

Antioxidants & redox signaling, 2011-03, Vol.14 (6), p.1039-1047

2011

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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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Crystallographic Snapshots of Cyanide- and Water-Bound C-Clusters from Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Biochemistry (Easton), 2009-08, Vol.48 (31), p.7432-7440

2009

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Investigations of Two Bidirectional Carbon Monoxide Dehydrogenases from Carboxydothermus hydrogenoformans by Protein Film Electrochemistry

Chembiochem : a European journal of chemical biology, 2013-09, Vol.14 (14), p.1845-1851

2013

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Metals and Their Scaffolds To Promote Difficult Enzymatic Reactions

Chemical reviews, 2006-08, Vol.106 (8), p.3317-3337

Ragsdale, Stephen W

2006

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The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order

The Journal of biological chemistry, 2015-04, Vol.290 (15), p.9322-9334

2015

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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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Nickel and the carbon cycle

Journal of inorganic biochemistry, 2007-11, Vol.101 (11), p.1657-1666

Ragsdale, Stephen W.

2007

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Water−Gas Shift Reaction Catalyzed by Redox Enzymes on Conducting Graphite Platelets

Journal of the American Chemical Society, 2009-10, Vol.131 (40), p.14154-14155

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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The heme-regulatory motif of nuclear receptor Rev-erbβ is a key mediator of heme and redox signaling in circadian rhythm maintenance and metabolism

The Journal of biological chemistry, 2017-07, Vol.292 (27), p.11280-11299

2017

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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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Life with Carbon Monoxide

Critical reviews in biochemistry and molecular biology, 2004-05, Vol.39 (3), p.165-195

Ragsdale, Stephen W.

2004

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Metal centers in the anaerobic microbial metabolism of CO and CO2

Metallomics, 2011-01, Vol.3 (8), p.797-815

2011

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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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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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Biochemical and Spectroscopic Studies of the Electronic Structure and Reactivity of a Methyl−Ni Species Formed on Methyl-Coenzyme M Reductase

Journal of the American Chemical Society, 2007-09, Vol.129 (36), p.11030-11032

2007

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An alcove at the acetyl-CoA synthase nickel active site is required for productive substrate CO binding and anaerobic carbon fixation

The Journal of biological chemistry, 2024-08, Vol.300 (8), p.107503, Article 107503

2024

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

The radical mechanism of biological methane synthesis by methyl-coenzyme M reductase

Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation

An unlikely heme chaperone confirmed at last

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

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

Thiol/Disulfide redox switches in the regulation of heme binding to proteins

Modulation of nuclear receptor function by cellular redox poise

Crystallographic Snapshots of Cyanide- and Water-Bound C-Clusters from Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

Investigations of Two Bidirectional Carbon Monoxide Dehydrogenases from Carboxydothermus hydrogenoformans by Protein Film Electrochemistry

Metals and Their Scaffolds To Promote Difficult Enzymatic Reactions

The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order

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

Nickel and the carbon cycle

Water−Gas Shift Reaction Catalyzed by Redox Enzymes on Conducting Graphite Platelets

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

The heme-regulatory motif of nuclear receptor Rev-erbβ is a key mediator of heme and redox signaling in circadian rhythm maintenance and metabolism

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

Life with Carbon Monoxide

Metal centers in the anaerobic microbial metabolism of CO and CO2

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

Biochemical and Spectroscopic Studies of the Electronic Structure and Reactivity of a Methyl−Ni Species Formed on Methyl-Coenzyme M Reductase

An alcove at the acetyl-CoA synthase nickel active site is required for productive substrate CO binding and anaerobic carbon fixation

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