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The Nature and Reactivity of Ferryl Heme in Compounds I and II

Accounts of chemical research, 2018-02, Vol.51 (2), p.427-435

2018

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Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase

Science (American Association for the Advancement of Science), 2014-07, Vol.345 (6193), p.193-197

2014

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In vitro evolution predicts emerging SARS-CoV-2 mutations with high affinity for ACE2 and cross-species binding

PLoS pathogens, 2022-07, Vol.18 (7), p.e1010733

2022

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A heme-binding domain controls regulation of ATP-dependent potassium channels

Proceedings of the National Academy of Sciences - PNAS, 2016-04, Vol.113 (14), p.3785-3790

2016

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Comparison of the Regulation, Metabolic Functions, and Roles in Virulence of the Glyceraldehyde-3-Phosphate Dehydrogenase Homologues gapA and gapB in Staphylococcus aureus

Infection and Immunity, 2010-12, Vol.78 (12), p.5223-5232

2010

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Molecular basis of sugar recognition by collectin-K1 and the effects of mutations associated with 3MC syndrome

BMC biology, 2015-04, Vol.13 (1), p.27-27, Article 27

2015

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The Tuberculosis Prodrug Isoniazid Bound to Activating Peroxidases

The Journal of biological chemistry, 2008-03, Vol.283 (10), p.6193-6200

2008

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XFEL Crystal Structures of Peroxidase Compound II

Angewandte Chemie International Edition, 2021-06, Vol.60 (26), p.14578-14585

International ed. in English, 2021

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Structure of the C1r–C1s interaction of the C1 complex of complement activation

Proceedings of the National Academy of Sciences - PNAS, 2018-01, Vol.115 (4), p.768-773

2018

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Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme

Nature communications, 2016-11, Vol.7 (1), p.13445-13445, Article 13445

2016

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Visualizing the protons in a metalloenzyme electron proton transfer pathway

Proceedings of the National Academy of Sciences - PNAS, 2020-03, Vol.117 (12), p.6484-6490

2020

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A mechanism for CO regulation of ion channels

Nature communications, 2018-03, Vol.9 (1), p.907-10, Article 907

2018

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Proton Delivery to Ferryl Heme in a Heme Peroxidase: Enzymatic Use of the Grotthuss Mechanism

Journal of the American Chemical Society, 2011-10, Vol.133 (39), p.15376-15383

2011

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Crystal structure of guaiacol and phenol bound to a heme peroxidase

The FEBS journal, 2012-05, Vol.279 (9), p.1632-1639

2012

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Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation

Proceedings of the National Academy of Sciences - PNAS, 2013-08, Vol.110 (34), p.13916-13920

2013

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The rise of neutron cryo‐crystallography

Acta crystallographica. Section D, Biological crystallography., 2018-08, Vol.74 (8), p.792-799

2018

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How is the distal pocket of a heme protein optimized for binding of tryptophan?

The FEBS journal, 2012-12, Vol.279 (24), p.4501-4509

2012

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The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex

Scientific reports, 2015-09, Vol.5 (1), p.13293-13293, Article 13293

2015

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Engineering the Substrate Specificity and Reactivity of a Heme Protein: Creation of an Ascorbate Binding Site in Cytochrome c Peroxidase

Biochemistry (Easton), 2008-12, Vol.47 (52), p.13933-13941

2008

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Activity of fructose-1,6-bisphosphatase from Campylobacter jejuni

Biochemistry and cell biology, 2020-07, Vol.98 (4), p.518-524

2020

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Combining X‐ray and neutron crystallography with spectroscopy

Acta crystallographica. Section D, Biological crystallography., 2017-02, Vol.73 (2), p.141-147

2017

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A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

Nature (London), 1995-11, Vol.378 (6555), p.416-419

1995

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Author Correction: A mechanism for CO regulation of ion channels

Nature communications, 2018-08, Vol.9 (1), p.3354-1, Article 3354

2018

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Crystal Structure of the Ascorbate Peroxidase−Salicylhydroxamic Acid Complex

Biochemistry (Easton), 2004-07, Vol.43 (27), p.8644-8651

2004

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Structure of Cu(I)-Bound DJ‑1 Reveals a Biscysteinate Metal Binding Site at the Homodimer Interface: Insights into Mutational Inactivation of DJ‑1 in Parkinsonism

Journal of the American Chemical Society, 2013-10, Vol.135 (43), p.15974-15977

2013

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The Nature and Reactivity of Ferryl Heme in Compounds I and II

Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase

In vitro evolution predicts emerging SARS-CoV-2 mutations with high affinity for ACE2 and cross-species binding

A heme-binding domain controls regulation of ATP-dependent potassium channels

Comparison of the Regulation, Metabolic Functions, and Roles in Virulence of the Glyceraldehyde-3-Phosphate Dehydrogenase Homologues gapA and gapB in Staphylococcus aureus

Molecular basis of sugar recognition by collectin-K1 and the effects of mutations associated with 3MC syndrome

The Tuberculosis Prodrug Isoniazid Bound to Activating Peroxidases

XFEL Crystal Structures of Peroxidase Compound II

Structure of the C1r–C1s interaction of the C1 complex of complement activation

Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme

Visualizing the protons in a metalloenzyme electron proton transfer pathway

A mechanism for CO regulation of ion channels

Proton Delivery to Ferryl Heme in a Heme Peroxidase: Enzymatic Use of the Grotthuss Mechanism

Crystal structure of guaiacol and phenol bound to a heme peroxidase

Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation

The rise of neutron cryo‐crystallography

How is the distal pocket of a heme protein optimized for binding of tryptophan?

The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex

Engineering the Substrate Specificity and Reactivity of a Heme Protein: Creation of an Ascorbate Binding Site in Cytochrome c Peroxidase

Activity of fructose-1,6-bisphosphatase from Campylobacter jejuni

Combining X‐ray and neutron crystallography with spectroscopy

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

Author Correction: A mechanism for CO regulation of ion channels

Crystal Structure of the Ascorbate Peroxidase−Salicylhydroxamic Acid Complex

Structure of Cu(I)-Bound DJ‑1 Reveals a Biscysteinate Metal Binding Site at the Homodimer Interface: Insights into Mutational Inactivation of DJ‑1 in Parkinsonism

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