Detalhe da pesquisa
1.
Stepwise assembly of the active site of [NiFe]-hydrogenase.
Nat Chem Biol
; 19(4): 498-506, 2023 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-36702959
2.
Stabilizing Monoatomic Two-Coordinate Bismuth(I) and Bismuth(II) Using a Redox Noninnocent Bis(germylene) Ligand.
J Am Chem Soc
; 146(9): 6025-6036, 2024 Mar 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-38408197
3.
Structural Determinants of the Catalytic Nia-L Intermediate of [NiFe]-Hydrogenase.
J Am Chem Soc
; 145(25): 13674-13685, 2023 06 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-37328284
4.
Reversible Glutamate Coordination to High-Valent Nickel Protects the Active Site of a [NiFe] Hydrogenase from Oxygen.
J Am Chem Soc
; 144(37): 17022-17032, 2022 09 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-36084022
5.
Catalytic and Spectroscopic Properties of the Halotolerant Soluble Methane Monooxygenase Reductase from Methylomonas methanica MC09.
Chembiochem
; 23(5): e202100592, 2022 03 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-34905639
6.
Crucial Role of the Chaperonin GroES/EL for Heterologous Production of the Soluble Methane Monooxygenase from Methylomonas methanica MC09.
Chembiochem
; 23(12): e202200195, 2022 06 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-35385600
7.
Changing the Reactivity of Zero- and Mono-Valent Germanium with a Redox Non-Innocent Bis(silylenyl)carborane Ligand.
Angew Chem Int Ed Engl
; 60(27): 14864-14868, 2021 Jun 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-33909944
8.
Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes.
Angew Chem Int Ed Engl
; 60(29): 15854-15862, 2021 07 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-33783938
9.
Shedding Light on Proton and Electron Dynamics in [FeFe] Hydrogenases.
J Am Chem Soc
; 142(12): 5493-5497, 2020 03 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-32125830
10.
Bis(silylene)-Stabilized Monovalent Nitrogen Complexes.
Angew Chem Int Ed Engl
; 59(49): 22043-22047, 2020 Dec 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-32841449
11.
Caught in the Hinact : Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2 -stable State of [FeFe] Hydrogenase.
Angew Chem Int Ed Engl
; 59(38): 16786-16794, 2020 09 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-32488975
12.
X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases.
Angew Chem Int Ed Engl
; 58(51): 18710-18714, 2019 12 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-31591784
13.
O2-Tolerant H2 Activation by an Isolated Large Subunit of a [NiFe] Hydrogenase.
Biochemistry
; 57(36): 5339-5349, 2018 09 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-30110155
14.
Enzymatic and spectroscopic properties of a thermostable [NiFe]hydrogenase performing H2-driven NAD+-reduction in the presence of O2.
Biochim Biophys Acta Bioenerg
; 1859(1): 8-18, 2018 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-28970007
15.
Single-Electron Transfer Reactions in Frustrated and Conventional Silylium Ion/Phosphane Lewis Pairs.
Angew Chem Int Ed Engl
; 57(46): 15267-15271, 2018 Nov 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-30178534
16.
Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.
Chem Sci
; 14(11): 2826-2838, 2023 Mar 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-36937599
17.
Stepwise conversion of the Cys6[4Fe-3S] to a Cys4[4Fe-4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase.
Chem Sci
; 14(40): 11105-11120, 2023 Oct 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-37860641
18.
High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase From Cupriavidus necator in Escherichia coli.
Front Microbiol
; 13: 894375, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-35572669
19.
Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production from Ralstonia eutropha H16 in Escherichia coli.
Microorganisms
; 9(6)2021 May 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-34073092
20.
In Vitro Assembly as a Tool to Investigate Catalytic Intermediates of [NiFe]-Hydrogenase.
ACS Catal
; 10(23): 13890-13894, 2020 Dec 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-33680535