Results 31 to 40 of about 36,091 (300)
Negative Cooperativity in the Nitrogenase Fe Protein Electron Delivery Cycle [PDF]
, 2016 Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to two ammonia (NH3) molecules through the participation of its two protein components, the MoFe and Fe proteins.
Antony, Edwin +11 more
core +2 more sources
Multireference protonation energetics of a dimeric model of nitrogenase iron-sulfur clusters [PDF]
, 2023 Characterizing the electronic structure of the iron--sulfur clusters in nitrogenase is necessary to understand their role in the nitrogen fixation process. One challenging task is to determine the protonation state of the intermediates in the nitrogen fixing cycle. Here, we use a dimeric iron--sulfur model to study relative energies of protonation at C,
arxiv +1 more source
Frontiers in Chemistry, 2021 Fast and reliable industrial production of ammonia (NH3) is fundamentally sustaining modern society. Since the early 20th Century, NH3 has been synthesized via the Haber–Bosch process, running at conditions of around 350–500°C and 100–200 times ...
Rebeca González-Cabaleiro +2 more
doaj +1 more source
Contrasted Reactivity to Oxygen Tensions in Frankia sp. Strain CcI3 throughout Nitrogen Fixation and Assimilation [PDF]
, 2014 Reconciling the irreconcilable is a primary struggle in aerobic nitrogen-fixing bacteria. Although nitrogenase is oxygen and reactive oxygen species-labile, oxygen tension is required to sustain respiration.
Beauchemin, Nicholas +6 more
core +4 more sources
Classifying the metal dependence of uncharacterized nitrogenases
Frontiers in Microbiology, 2013 Nitrogenase enzymes have evolved complex iron-sulfur (Fe-S) containing cofactors that most commonly contain molybdenum (MoFe, Nif) as a heterometal but also exist as vanadium (VFe, Vnf) and heterometal independent (Fe-only, Anf) forms.
Shawn E Mcglynn +3 more
doaj +1 more source
Activation and Protonation of Dinitrogen at the FeMo-Cofactor of Nitrogenase [PDF]
J. Chem. Phys. 123, 074306 (2005), 2005 The protonation of N2 bound to the active center of nitrogenase has been investigated using state-of-the-art DFT calculations. Dinitrogen in the bridging mode is activated by forming two bonds to Fe sites, which results in a reduction of the energy for the first hydrogen transfer by 123 kJ/mol.
arxiv +1 more source
Scientific Reports, 2022 Biological nitrogen fixation (BNF) is the reduction of N2 into NH3 in a group of prokaryotes by an extremely O2-sensitive protein complex called nitrogenase. Transfer of the BNF pathway directly into plants, rather than by association with microorganisms,
Lucía Payá-Tormo +11 more
doaj +1 more source
Strong Electron Correlation in Nitrogenase Cofactor, FeMoco [PDF]
J. M. Montgomery and D. A. Mazziotti, J. Phys. Chem. A 2018, 2018 FeMoco, MoFe$_7$S$_9$C, has been shown to be the active catalytic site for the reduction of nitrogen to ammonia in the nitrogenase protein. An understanding of its electronic structure including strong electron correlation is key to designing mimic catalysts capable of ambient nitrogen fixation. Active spaces ranging from [54, 54] to [65, 57] have been
arxiv +1 more source
NifA is the master regulator of both nitrogenase systems in Rhodobacter capsulatus
MicrobiologyOpen, 2019 Rhodobacter capsulatus fixes atmospheric nitrogen (N2) by a molybdenum (Mo)‐nitrogenase and a Mo‐free iron (Fe)‐nitrogenase, whose production is induced or repressed by Mo, respectively. At low nanomolar Mo concentrations, both isoenzymes are synthesized
Lisa Demtröder +4 more
doaj +1 more source
Molecular Plant-Microbe Interactions, 2016 Bradyrhizobium sp. strain DOA9 contains two copies of the nifDK genes, nifDKc, located on the chromosome, and nifDKp, located on a symbiotic megaplasmid.
Jenjira Wongdee +8 more
doaj +1 more source