Results 11 to 20 of about 5,806,549 (219)
Cellular differentiation and nitrogenase activity in the cyanobacteriumAnabaena [PDF]
Biologia Plantarum, 1982 Nitrogenase activity at periods of differentiation of heterocysts and akinetes was assayed by the acetylene reduction technique. There was no nitrogenase activity in ammoniumgrown, non-heterocystousAnabaena sp.; the activity appeared only after a lag-phase of about 17 – 21 h after the ammonium-grown culture had been transferred to medium free of ...
A. S. Ahluwalia, H. D. Kumar
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Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase [PDF]
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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Azotobacter vinelandii Nitrogenase Activity, Hydrogen Production, and Response to Oxygen Exposure. [PDF]
Appl Environ Microbiol, 2018 A. vinelandii has been a focus of intense research for over 100 years. It has been investigated for a variety of functions, including agricultural fertilization and hydrogen production. All of these endeavors are centered around
Natzke J, Noar J, Bruno-Bárcena JM.
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Acta Scientiarum. Agronomy, 2021 The initial development of common bean plants (Phaseolus vulgaris L.) relying on symbiotic nitrogen (N) can be limited by delayed active N2 fixation, requiring supplemental N which in turn may inhibit the symbiosis.
Bárbara Cavalheiro Zoffoli +3 more
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Rethinking the Nitrogenase Mechanism: Activating the Active Site [PDF]
Joule, 2019 Metalloenzymes called nitrogenases (N2ases) harness the reactivity of transition metals to reduce N2 to NH3. Specifically, N2ases feature a multimetallic active site, called a cofactor, which binds and reduces N2. The seven Fe centers and one additional metal center (Mo, V, or Fe) that make up the cofactor are all potential substrate binding sites ...
Buscagan, Trixia M., Rees, Douglas C.
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Diurnal Variations of Nitrogenase Activity in the Field [PDF]
Applied Microbiology, 1974 Nitrogenase activity was determined in situ by repeated assays at regular intervals to compare the patterns of diurnal variations occurring in a rice field, a grassland, and a peanut field. In the rice field only one peak occurred (mid-day), whereas the other systems exhibited typical two-peak patterns, which were suspected to be induced by climatic ...
J P, Balandreau +2 more
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Hydrogenase activity in Rhodopseudomonas capsulata: relationship with nitrogenase activity [PDF]
Journal of Bacteriology, 1980 Hydrogenase activity was found in cells of Rhodopseudomonas capsulata strain B10 cultured under a variety of growth conditions either anaerobically in the light or aerobically in the dark. The highest activities were found routinely in cells grown in the presence of H2. The hydrogenase of R.
A, Colbeau, B C, Kelley, P M, Vignais
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Activation and protonation of dinitrogen at the FeMo cofactor of nitrogenase [PDF]
The Journal of Chemical Physics, 2005 The protonation of N2 bound to the active center of nitrogenase has been investigated using state-of-the-art density-functional theory 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 123kJ∕mol.
Kästner, J., Hemmen, S., Blöchl, P.
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Regulatory response to a hybrid ancestral nitrogenase in Azotobacter vinelandii
Microbiology Spectrum, 2023 Biological nitrogen fixation, the microbial reduction of atmospheric nitrogen to bioavailable ammonia, represents both a major limitation on biological productivity and a highly desirable engineering target for synthetic biology. However, the engineering
Alex J. Rivier +4 more
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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
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