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Browsing by Author "Bjornsson, Ragnar"
Now showing items 1-11 of 11
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(Royal Society of Chemistry (RSC), 2017)An investigation of the active site cofactors of the molybdenum and vanadium nitrogenases (FeMoco and FeVco) was performed using high-resolution X-ray spectroscopy. Synthetic heterometallic iron–sulfur cluster models and density functional theory ... -
(Elsevier BV, 2017-03)The conformational preference of the cyano group of the 1-cyano-1-silacyclohexane was studied experimentally by means of gas electron diffraction (GED) and dynamic nuclear magnetic resonance (DNMR) as well as by quantum chemical (QC) calculations ...
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(Beilstein Institut, 2018-02-14)In the current contribution we present a comprehensive study on the heteronuclear carbonyl complex H2FeRu3(CO)13 covering its low energy electron induced fragmentation in the gas phase through dissociative electron attachment (DEA) and dissociative ...
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(Royal Society of Chemistry (RSC), 2017)In single electron collisions with the heteronuclear metal carbonyl compound HFeCo3(CO)12 we observe the formation of long-lived negative ion states up to about 20 eV, 11 eV above its ionization energy. These transient negative ions (TNIs) relax through ...
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(Royal Society of Chemistry (RSC), 2019-10-15)Molybdenum nitrogenase is one of the most intriguing metalloenzymes in nature, featuring an exotic iron-molybdenum-sulfur cofactor, FeMoco, whose mode of action remains elusive. In particular, the molecular and electronic structure of the N2-binding ...
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(American Chemical Society (ACS), 2017-07-21)Here we present a combined experimental and theoretical study on the fragmentation of o- and p-tetrafluorohydroquinone upon low energy electron attachment. Despite an identical ring-skeleton and identical functional groups in these constitutional ...
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(Royal Society of Chemistry (RSC), 2018)A new 1.2 Å crystal structure of vanadium nitrogenase, isolated under turnover conditions, recently revealed a light atom ligand (OH or NH) replacing the bridging S2B sulfide of the FeV cofactor. QM/MM calculations on the new structure now reveal the ...
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(American Chemical Society (ACS), 2017-10-20)Nitrogenase is one of the most fascinating enzymes in nature, being responsible for all biological nitrogen reduction. Despite decades of research, it is among the enzymes in bioinorganic chemistry whose mechanism is the most poorly understood. The ...
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(American Chemical Society (ACS), 2020-08-05)The nitrogenase enzymes are responsible for all biological nitrogen reduction. How this is accomplished at the atomic level, however, has still not been established. The molybdenum-dependent nitrogenase has been extensively studied and is the most ...
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Revisiting the Mössbauer Isomer Shifts of the FeMoco Cluster of Nitrogenase and the Cofactor Charge (American Chemical Society (ACS), 2017-01-10)Despite decades of research, the structure–activity relationship of nitrogenase is still not understood. Only recently was the full molecular structure of the FeMo cofactor (FeMoco) revealed, but the charge and metal oxidation states of FeMoco have ...
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(American Chemical Society (ACS), 2018)A combination of two elements’ (Au, Zn) X-ray absorption spectroscopy (XAS) and time-dependent density functional theory (TD-DFT) allowed the elucidation of differential substitution pathways of Au(I) and Au(III) compounds reacting with biologically ...
Now showing items 1-11 of 11