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A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

Nature communications, 2023-06, Vol.14 (1), p.3416-3416, Article 3416

2023

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Reverse protein engineering of a novel 4‐domain copper nitrite reductase reveals functional regulation by protein–protein interaction

The FEBS journal, 2021-01, Vol.288 (1), p.262-280

2021

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Structures of protein-protein complexes involved in electron transfer

Nature (London), 2013-04, Vol.496 (7443), p.123-126

2013

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Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases

Proceedings of the National Academy of Sciences - PNAS, 2022-07, Vol.119 (30), p.1-e2205664119

2022

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Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis

Chemical science (Cambridge), 2020-01, Vol.11 (46), p.12485-12492

2020

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Atomic Resolution Structures of Resting-State, Substrate- and Product-Complexed Cu-Nitrite Reductase Provide Insight into Catalytic Mechanism

Proceedings of the National Academy of Sciences - PNAS, 2005-08, Vol.102 (34), p.12041-12046

2005

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Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis

ACS catalysis, 2019-07, Vol.9 (7), p.6087-6099

2019

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Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal

IUCrJ, 2016-07, Vol.3 (Pt 4), p.271-281

2016

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Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase

Biochemistry (Easton), 2011-05, Vol.50 (19), p.4121-4131

2011

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New horizons in structure-function studies of copper nitrite reductase

Coordination chemistry reviews, 2022-06, Vol.460, p.214463, Article 214463

2022

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An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase

IUCrJ, 2018-01, Vol.5 (Pt 1), p.22-31

2018

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Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography

IUCrJ, 2019-07, Vol.6 (Pt 4), p.761-772

2019

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Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes

IUCrJ, 2020-05, Vol.7 (Pt 3), p.557-565

2020

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Enzyme catalysis captured using multiple structures from one crystal at varying temperatures

IUCrJ, 2018-05, Vol.5 (Pt 3), p.283-292

2018

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Demonstration of Proton-coupled Electron Transfer in the Copper-containing Nitrite Reductases

The Journal of biological chemistry, 2009-09, Vol.284 (38), p.25973-25983

2009

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Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins

Proceedings of the National Academy of Sciences - PNAS, 2011-09, Vol.108 (38), p.15780-15785

2011

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Identification of a tyrosine switch in copper-haem nitrite reductases

IUCrJ, 2018-07, Vol.5 (Pt 4), p.510-518

2018

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Identification of the Proton Channel to the Active Site Type 2 Cu Center of Nitrite Reductase: Structural and Enzymatic Properties of the His254Phe and Asn90Ser Mutants

Biochemistry (Easton), 2008-12, Vol.47 (51), p.13547-13553

2008

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Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii

Biochemical journal, 2012-06, Vol.444 (2), p.219-226

2012

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Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes xylosoxidans and the Active Site Mutant Asp92Glu

Journal of molecular biology, 2003-04, Vol.328 (2), p.429-438

2003

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Electron transfer and half-reactivity in nitrogenase

Biochemical Society transactions, 2011-02, Vol.39 (1), p.201

2011

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Fresh insight to functioning of selected enzymes of the nitrogen cycle

Current opinion in chemical biology, 2016-04, Vol.31, p.103-112

2016

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Active site structures and the redox properties of blue copper proteins: atomic resolution structure of azurin II and electronic structure calculations of azurin, plastocyanin and stellacyanin

Dalton transactions : an international journal of inorganic chemistry, 2006-01 (25), p.3067-3076

2006

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Structure−Function Relationships of Alternative Nitrogenases

Chemical reviews, 1996, Vol.96 (7), p.3013-3030

Eady, Robert R

1996

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Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase

Nature communications, 2014-07, Vol.5 (1), p.4395-4395, Article 4395

2014

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A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

Reverse protein engineering of a novel 4‐domain copper nitrite reductase reveals functional regulation by protein–protein interaction

Structures of protein-protein complexes involved in electron transfer

Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases

Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis

Atomic Resolution Structures of Resting-State, Substrate- and Product-Complexed Cu-Nitrite Reductase Provide Insight into Catalytic Mechanism

Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis

Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal

Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase

New horizons in structure-function studies of copper nitrite reductase

An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase

Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography

Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes

Enzyme catalysis captured using multiple structures from one crystal at varying temperatures

Demonstration of Proton-coupled Electron Transfer in the Copper-containing Nitrite Reductases

Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins

Identification of a tyrosine switch in copper-haem nitrite reductases

Identification of the Proton Channel to the Active Site Type 2 Cu Center of Nitrite Reductase: Structural and Enzymatic Properties of the His254Phe and Asn90Ser Mutants

Characterization of a novel copper-haem c dissimilatory nitrite reductase from Ralstonia pickettii

Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes xylosoxidans and the Active Site Mutant Asp92Glu

Electron transfer and half-reactivity in nitrogenase

Fresh insight to functioning of selected enzymes of the nitrogen cycle

Active site structures and the redox properties of blue copper proteins: atomic resolution structure of azurin II and electronic structure calculations of azurin, plastocyanin and stellacyanin

Structure−Function Relationships of Alternative Nitrogenases

Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase

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