Results 61 to 70 of about 28,179 (272)

Nitrogenase Bioelectrocatalysis: ATP-Independent Ammonia Production Using a Redox Polymer/MoFe Protein System

open access: yesACS Catalysis, 2020
Nitrogenase is the only biological catalyst that is known to be able to convert nitrogen gas to ammonia.
Y. Lee   +4 more
semanticscholar   +1 more source

Nitrogenase: A Draft Mechanism [PDF]

open access: yesAccounts of Chemical Research, 2013
Biological nitrogen fixation, the reduction of N(2) to two NH(3) molecules, supports more than half the human population. The predominant form of the enzyme nitrogenase, which catalyzes this reaction, comprises an electron-delivery Fe protein and a catalytic MoFe protein.
Dennis R. Dean   +3 more
openaire   +3 more sources

Cross-Activation of Two Nitrogenase Gene Clusters by CnfR1 or CnfR2 in the Cyanobacterium Anabaena variabilis

open access: yesMicrobiology Spectrum, 2021
In Anabaena variabilis, the nif1 genes, which are activated by CnfR1, produce a Mo-nitrogenase that is expressed only in heterocysts. Similarly, the nif2 genes, which are activated by CnfR2, make a Mo-nitrogenase that is expressed only in anaerobic ...
Brenda S. Pratte, Teresa Thiel
doaj   +1 more source

Carbon substrate re‐orders relative growth of a bacterium using Mo‐, V‐, or Fe‐nitrogenase for nitrogen fixation

open access: yesEnvironmental Microbiology, 2020
Summary Biological nitrogen fixation is catalyzed by the molybdenum (Mo), vanadium (V) and iron (Fe)‐only nitrogenase metalloenzymes. Studies with purified enzymes have found that the ‘alternative’ V‐ and Fe‐nitrogenases generally reduce N2 more slowly ...
K. Luxem   +4 more
semanticscholar   +1 more source

Electronic landscape of the P-cluster of nitrogenase as revealed through many-electron quantum wavefunction simulations [PDF]

open access: yesNature Chemistry, 2018
The electronic structure of the nitrogenase metal cofactors is central to nitrogen fixation. However, the P-cluster and FeMo cofactor, each containing eight Fe atoms, have eluded detailed characterization of their electronic properties.
Zhendong Li   +3 more
semanticscholar   +1 more source

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

open access: yesChemBioChem, 2020
AbstractThe 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. Nitrogenase‐like enzymes involved in coenzyme F430 and chlorophyll biosynthesis utilize the highly homologous reductases ...
Jan Jasper   +6 more
openaire   +4 more sources

Antenna Modification Leads to Enhanced Nitrogenase Activity in a High Light-Tolerant Cyanobacterium

open access: yesmBio, 2021
Biological nitrogen fixation is an energy-intensive process that contributes significantly toward supporting life on this planet. Among nitrogen-fixing organisms, cyanobacteria remain unrivaled in their ability to fuel the energetically expensive ...
Anindita Bandyopadhyay   +4 more
doaj   +1 more source

The structure of vanadium nitrogenase reveals an unusual bridging ligand

open access: yesNature Chemical Biology, 2017
Nitrogenases catalyze the reduction of N2 gas to ammonium at a complex heterometallic cofactor. Most commonly this is the FeMo cofactor (FeMoco), a [Mo:7Fe:9S:C] cluster whose exact reactivity and substrate binding mode remain unknown.
D. Sippel, O. Einsle
semanticscholar   +1 more source

Bioinspired Design of Heterogenous Single‐Atomic‐Site Catalysts for Electrocatalysis and Photocatalysis

open access: yesAdvanced Materials, EarlyView.
This review gives a summary on the representative bioinspired single‐atomic‐site catalysts (SACs) and their applications in heterogeneous electrocatalysis and photocatalysis. The fundamentals of bioinspired design strategies are systematically discussed in the context of the first shell coordination, the second/long‐range coordination, and the outer ...
Ying Wang   +4 more
wiley   +1 more source

Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for N2 reduction

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2018
Significance This report critically evaluates the mechanism by which nitrogenase cleaves the N≡N triple bond. It assesses the thermodynamic driving force provided by the accompanying, apparently “wasteful,” reductive elimination of an H2, and explains ...
S. Raugei, L. Seefeldt, B. Hoffman
semanticscholar   +1 more source

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