Results 11 to 20 of about 28,179 (272)
Biosynthesis of Nitrogenase Cofactors [PDF]
Chemical Reviews, 2020 Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity. The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component.
Stefan Burén +3 more
semanticscholar +5 more sources
PII protein is essential for transcriptional regulation of anf gene cluster for iron-only nitrogenase in Rhodopseudomonas palustris [PDF]
Applied and Environmental MicrobiologyIn addition to catalyzing the biological nitrogen fixation, iron-only (Fe-only) nitrogenase is also able to reduce carbon dioxide (CO2) to formate (HCOO−) and methane (CH4).
Yan Zeng +7 more
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NifA is the master regulator of both nitrogenase systems in Rhodobacter capsulatus
MicrobiologyOpen, 2019 Rhodobacter capsulatus fixes atmospheric nitrogen (N2) by a molybdenum (Mo)‐nitrogenase and a Mo‐free iron (Fe)‐nitrogenase, whose production is induced or repressed by Mo, respectively. At low nanomolar Mo concentrations, both isoenzymes are synthesized
Lisa Demtröder +4 more
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Electron Transfer in Nitrogenase.
Chemical Reviews, 2020 Nitrogenase is the only enzyme capable of reducing N2 to NH3. This challenging reaction requires the coordinated transfer of multiple electrons from the reductase, Fe-protein, to the catalytic component, MoFe-protein, in an ATP-dependent fashion.
H. Rutledge, F. Tezcan
semanticscholar +5 more sources
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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Energy Transduction in Nitrogenase. [PDF]
Accounts of Chemical Research, 2018 Nitrogenase is a complicated two-component enzyme system that uses ATP binding and hydrolysis energy to achieve one of the most difficult chemical reactions in nature, the reduction of N2 to NH3.
L. Seefeldt +6 more
semanticscholar +5 more sources
Frontiers in Microbiology, 2019 Since nitrogenase is extremely vulnerable to oxygen, aerobic or micro-aerobic nitrogen-fixing organisms need to create anaerobic microenvironments in the cells for diazotrophic growth, which would be one of the major barriers to express active ...
Aoi Nonaka +7 more
doaj +2 more sources
Structural insights into the iron nitrogenase complex
bioRxiv, 2023 Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO_2) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon ...
Frederik V. Schmidt +6 more
semanticscholar +1 more source
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
openaire +3 more sources
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
doaj +1 more source