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On the Shoulders of Giants-Reaching for Nitrogenase

Molecules (Basel, Switzerland), 2023-12, Vol.28 (24), p.7959

Einsle, Oliver

2023

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Nitrogenase FeMo cofactor: an atomic structure in three simple steps

Journal of biological inorganic chemistry, 2014-08, Vol.19 (6), p.737-745

Einsle, Oliver

2014

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The structure of vanadium nitrogenase reveals an unusual bridging ligand

Nature chemical biology, 2017-09, Vol.13 (9), p.956-960

2017

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Structural Enzymology of Nitrogenase Enzymes

Chemical reviews, 2020-06, Vol.120 (12), p.4969-5004

2020

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CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution

Angewandte Chemie International Edition, 2020-12, Vol.59 (52), p.23626-23630

International ed. in English, 2020

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Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase

Science (American Association for the Advancement of Science), 2014-09, Vol.345 (6204), p.1620-1623

2014

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A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII)

Journal of the American Chemical Society, 2016-01, Vol.138 (1), p.239-247

2016

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A bound reaction intermediate sheds light on the mechanism of nitrogenase

Science (American Association for the Advancement of Science), 2018-03, Vol.359 (6383), p.1484-1489

2018

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Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation

Nature communications, 2023-08, Vol.14 (1), p.5190-5190, Article 5190

2023

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Maximale Reduktionskraft voraus: mehr als die biologische Variante

Biospektrum, 2024-05, Vol.30 (3), p.268-272

Einsle, Oliver

2024

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Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

Science (American Association for the Advancement of Science), 2011-11, Vol.334 (6058), p.940-940

2011

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Catalysis and structure of nitrogenases

Current opinion in structural biology, 2023-12, Vol.83, p.102719-102719, Article 102719

Einsle, Oliver

2023

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Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

Nature communications, 2016-03, Vol.7 (1), p.10902-10902, Article 10902

2016

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Selective Sirt2 inhibition by ligand-induced rearrangement of the active site

Nature communications, 2015-02, Vol.6 (1), p.6263-6263, Article 6263

2015

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The Fe-V Cofactor of Vanadium Nitrogenase Contains an Interstitial Carbon Atom

Angewandte Chemie (International ed.), 2015-11, Vol.54 (45), p.13249-13252

International ed. in English, 2015

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Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra

Nature communications, 2024-05, Vol.15 (1), p.4041-4041, Article 4041

2024

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The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry

Journal of biological inorganic chemistry, 2015-03, Vol.20 (2), p.447-460

2015

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Identification of a spin-coupled Mo( iii ) in the nitrogenase iron–molybdenum cofactor

Chemical science (Cambridge), 2014-01, Vol.5 (8), p.3096-3103

2014

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Establishing a Thermodynamic Landscape for the Active Site of Mo-Dependent Nitrogenase

Journal of the American Chemical Society, 2019-10, Vol.141 (43), p.17150-17157

2019

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Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure–Activity Relationship Study

Journal of medicinal chemistry, 2016-02, Vol.59 (4), p.1599-1612

2016

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A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I

Nature communications, 2019-06, Vol.10 (1), p.2551-9, Article 2551

2019

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Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber

Scientific reports, 2017-07, Vol.7 (1), p.6179-11, Article 6179

2017

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Histidine-Gated Proton-Coupled Electron Transfer to the CuA Site of Nitrous Oxide Reductase

Journal of the American Chemical Society, 2021-01, Vol.143 (2), p.830-838

2021

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Structure-Based Development of an Affinity Probe for Sirtuin 2

Angewandte Chemie (International ed.), 2016-02, Vol.55 (6), p.2252-2256

2016

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Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures

Proceedings of the National Academy of Sciences - PNAS, 2018-03, Vol.115 (13), p.3350-3355

2018

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On the Shoulders of Giants-Reaching for Nitrogenase

Nitrogenase FeMo cofactor: an atomic structure in three simple steps

The structure of vanadium nitrogenase reveals an unusual bridging ligand

Structural Enzymology of Nitrogenase Enzymes

CO Binding to the FeV Cofactor of CO‐Reducing Vanadium Nitrogenase at Atomic Resolution

Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase

A Conformational Switch Triggers Nitrogenase Protection from Oxygen Damage by Shethna Protein II (FeSII)

A bound reaction intermediate sheds light on the mechanism of nitrogenase

Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation

Maximale Reduktionskraft voraus: mehr als die biologische Variante

Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

Catalysis and structure of nitrogenases

Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

Selective Sirt2 inhibition by ligand-induced rearrangement of the active site

The Fe-V Cofactor of Vanadium Nitrogenase Contains an Interstitial Carbon Atom

Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra

The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry

Identification of a spin-coupled Mo( iii ) in the nitrogenase iron–molybdenum cofactor

Establishing a Thermodynamic Landscape for the Active Site of Mo-Dependent Nitrogenase

Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure–Activity Relationship Study

A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I

Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber

Histidine-Gated Proton-Coupled Electron Transfer to the CuA Site of Nitrous Oxide Reductase

Structure-Based Development of an Affinity Probe for Sirtuin 2

Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures

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