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Nickel-based Enzyme Systems

The Journal of biological chemistry, 2009-07, Vol.284 (28), p.18571-18575

Ragsdale, Stephen W.

2009

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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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Selective Visible-Light-Driven CO2 Reduction on a p‑Type Dye-Sensitized NiO Photocathode

Journal of the American Chemical Society, 2014-10, Vol.136 (39), p.13518-13521

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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X‑ray Absorption Spectroscopy Reveals an Organometallic Ni–C Bond in the CO-Treated Form of Acetyl-CoA Synthase

Biochemistry (Easton), 2017-03, Vol.56 (9), p.1248-1260

2017

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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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One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography

Proceedings of the National Academy of Sciences - PNAS, 2016-01, Vol.113 (2), p.320-325

2016

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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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Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases

Biochimica et biophysica acta, 2012-11, Vol.1824 (11), p.1291-1298

2012

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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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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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Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis

Journal of the American Chemical Society, 2011-04, Vol.133 (15), p.5626-5628

2011

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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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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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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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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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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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Visible light-driven CO2 reduction by enzyme coupled CdS nanocrystals

Chemical communications (Cambridge, England), 2012-01, Vol.48 (1), p.58-60

2012

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Dual Roles of an Essential Cysteine Residue in Activity of a Redox-regulated Bacterial Transcriptional Activator

The Journal of biological chemistry, 2008-10, Vol.283 (42), p.28721-28728

2008

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Nickel-based Enzyme Systems

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

Selective Visible-Light-Driven CO2 Reduction on a p‑Type Dye-Sensitized NiO Photocathode

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

X‑ray Absorption Spectroscopy Reveals an Organometallic Ni–C Bond in the CO-Treated Form of Acetyl-CoA Synthase

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

One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography

Metals and Their Scaffolds To Promote Difficult Enzymatic Reactions

Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases

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

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

Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis

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

Metal centers in the anaerobic microbial metabolism of CO and CO2

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

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

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

Visible light-driven CO2 reduction by enzyme coupled CdS nanocrystals

Dual Roles of an Essential Cysteine Residue in Activity of a Redox-regulated Bacterial Transcriptional Activator

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