Results 11 to 20 of about 11,660 (194)
Notulae Botanicae Horti Agrobotanici Cluj-NapocaNitrogenase is a complicated enzyme that actives the ATP-dependent reduction of dinitrogen (N2) to ammonia (NH3). The aim of this manuscript is to review the nitrogenase evolution with considering nitrogenase, structure of nitrogenase, action mechanism ...
Wenli SUN, Mohamad Hesam SHAHRAJABIAN
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The Spectroscopy of Nitrogenases [PDF]
Chemical Reviews, 2020 Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and a series of iron-sulfur clusters to perform this reaction, culminating at the FeMco active site (M = Mo, V, Fe), which is capable of binding and reducing N2 to 2NH3. In this review,
Casey Van Stappen +6 more
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The photoreduction of nitrogenase [PDF]
Biochemical Journal, 1993 The photoreduction, without reductant dithionite, of N2 to NH3 or acetylene to ethylene catalysed by nitrogenase in the presence of Mg2+. ATP, eosin and NADH in the light has been established. There is an optimum NADH concentration for each particular eosin concentration.
, Druzhinin SYu +3 more
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Metalloclusters of the nitrogenases [PDF]
European Journal of Biochemistry, 1992 Biological nitrogen fixation, the reduction of dinitrogen to ammonia, is catalysed by nitrogenases. These enzymes are found in relatively few groups of bacteria and until recently it appeared that N2 fixation occurred by a single route involving a molybdenum-containing enzyme.
B E, Smith, R R, Eady
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Nitrogenase resurrection and the evolution of a singular enzymatic mechanism
eLife, 2023 The planetary biosphere is powered by a suite of key metabolic innovations that emerged early in the history of life. However, it is unknown whether life has always followed the same set of strategies for performing these critical tasks.
Amanda K Garcia +6 more
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An alternative path for the evolution of biological nitrogen fixation
Frontiers in Microbiology, 2011 Nitrogenase catalyzed nitrogen fixation is the process by which life converts dinitrogen gas into fixed nitrogen in the form of bioavailable ammonia. The most common form of nitrogenase today requires a complex metal cluster containing molybdenum (Mo ...
Eric S Boyd +2 more
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Food and Energy Security, 2023 Soybean is a rich source of protein and oil for humans. It forms a symbiotic association with rhizobia to fix atmospheric nitrogen for its growth and development. Rhizobial type‐III effectors act as important signaling molecules in symbiosis.
Chao Ma +9 more
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Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster
eLife, 2022 The nitrogenase Fe protein mediates ATP-dependent electron transfer to the nitrogenase MoFe protein during nitrogen fixation, in addition to catalyzing MoFe protein-independent substrate (CO2) reduction and facilitating MoFe protein metallocluster ...
Trixia M Buscagan +2 more
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2013 Nitrogenase contains two unique metalloclusters: the P-cluster and the M-cluster. The assembly processes of P- and M-clusters are arguably the most complicated processes in bioinorganic chemistry. There is considerable interest in decoding the biosynthetic mechanisms of the P- and M-clusters, because these clusters are not only biologically important ...
Hu, Yilin, Ribbe, Markus W.
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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
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