Results 11 to 20 of about 6,680 (190)

Nitrogenase and homologs. [PDF]

open access: yesJBIC Journal of Biological Inorganic Chemistry, 2015
Nitrogenase catalyzes biological nitrogen fixation, a key step in the global nitrogen cycle. Three homologous nitrogenases have been identified to date, along with several structural and/or functional homologs of this enzyme that are involved in ...
Hu, Yilin, Ribbe, Markus W
core   +6 more sources

Nitrogenase

open access: yes, 2011
Nitrogenase catalyzes the enzymatic reduction of atmospheric dinitrogen to ammonia during the process of biological nitrogen fixation. Nitrogenase consists of two component metalloproteins, the iron (Fe-) protein and the molybdenum-iron (MoFe-) protein ...
Howard, James B.   +9 more
core   +2 more sources

Crystallization of Nitrogenase Proteins

open access: yes, 2018
Nitrogenase is the only known enzymatic system capable of reducing atmospheric dinitrogen to ammonia. This unique reaction requires tightly choreographed interactions between the nitrogenase component proteins, the molybdenum–iron (MoFe)- and iron (Fe ...
Spatzal, Thomas   +5 more
core   +4 more sources

Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase

open access: yesChemBioChem, 2020
The engineering of transgenic organisms with the ability to fix nitrogen is an attractive possibility. However, oxygen sensitivity of nitrogenase, mainly conferred by the reductase component (NifH)2, is an imminent problem.
Oliver Einsle   +13 more
core   +4 more sources

The Spectroscopy of Nitrogenases [PDF]

open access: yesChemical 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
openaire   +3 more sources

The photoreduction of nitrogenase [PDF]

open access: yesBiochemical 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
openaire   +2 more sources

Metalloclusters of the nitrogenases [PDF]

open access: yesEuropean 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
openaire   +2 more sources

Functional Nitrogenase Cofactor Maturase NifB in Mitochondria and Chloroplasts of Nicotiana benthamiana

open access: yesmBio, 2022
Engineering plants to synthesize nitrogenase and assimilate atmospheric N2 will reduce crop dependency on industrial N fertilizers. This technology can be achieved by expressing prokaryotic nitrogen fixation gene products for the assembly of a functional
Xi Jiang   +8 more
doaj   +1 more source

Nitrogenase resurrection and the evolution of a singular enzymatic mechanism

open access: yeseLife, 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
doaj   +1 more source

Rhodobacter capsulatus AnfA is essential for production of Fe‐nitrogenase proteins but dispensable for cofactor biosynthesis and electron supply

open access: yesMicrobiologyOpen, 2020
The photosynthetic α‐proteobacterium Rhodobacter capsulatus reduces and thereby fixes atmospheric dinitrogen (N2) by a molybdenum (Mo)‐nitrogenase and an iron‐only (Fe)‐nitrogenase.
Lisa Demtröder   +2 more
doaj   +1 more source

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