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Browsing by Author "Benediktsson, Bardi"
Now showing items 1-4 of 4
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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 ... -
(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 ...
Now showing items 1-4 of 4