Results 31 to 40 of about 28,179 (272)

Nitrogenase Fe Protein: A Multi-Tasking Player in Substrate Reduction and Metallocluster Assembly

open access: yesMolecules, 2022
The Fe protein of nitrogenase plays multiple roles in substrate reduction and metallocluster assembly. Best known for its function to transfer electrons to its catalytic partner during nitrogenase catalysis, the Fe protein is also a key player in the ...
Markus W. Ribbe   +7 more
doaj   +1 more source

Structural Enzymology of Nitrogenase Enzymes.

open access: yesChemical Reviews, 2020
The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography involving two component proteins, MgATP and reductant. At center stage of this process resides the active site cofactor, a complex metallocluster organized around a ...
O. Einsle, D. Rees
semanticscholar   +1 more source

Exploiting genetic diversity and gene synthesis to identify superior nitrogenase NifH protein variants to engineer N2-fixation in plants

open access: yesCommunications Biology, 2021
Engineering nitrogen fixation in eukaryotes requires high expression of functional nitrogenase structural proteins, a goal that has not yet been achieved.
Xi Jiang   +8 more
semanticscholar   +1 more source

Purple sulfur bacteria fix N2 via molybdenum-nitrogenase in a low molybdenum Proterozoic ocean analogue

open access: yesNature Communications, 2021
Biological N2 fixation was key to the expansion of life on early Earth. The N2-fixing microorganisms and the nitrogenase type used in the Proterozoic are unknown, although it has been proposed that the canonical molybdenum-nitrogenase was not used due to
M. Philippi   +11 more
semanticscholar   +1 more source

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.
G I Likhtenstein   +3 more
openaire   +3 more sources

Reconstruction of Nitrogenase Predecessors Suggests Origin from Maturase-Like Proteins

open access: yesbioRxiv, 2021
The evolution of biological nitrogen fixation, uniquely catalyzed by nitrogenase enzymes, has been one of the most consequential biogeochemical innovations over life’s history.
Amanda K. Garcia   +2 more
semanticscholar   +1 more source

Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster

open access: yeseLife, 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
doaj   +1 more source

Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase

open access: yesScience, 2020
Delicate dance becomes a ballet The enzyme nitrogenase uses adenosine triphosphate and several unusual iron-sulfur cofactors to pump electrons into typically inert dinitrogen (N2), providing protons along the way.
W. Kang   +4 more
semanticscholar   +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

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

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