Results 1 to 10 of about 47,392 (275)

Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii

Nature, 1992
exaly  

Nitrogenase Activity in Heterocysts of Blue–Green Algae

Nature, 1969
exaly  

Nitrogenase resurrection and the evolution of a singular enzymatic mechanism

eLife, 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, Derek F Harris, Alex J Rivier, Brooke M Carruthers, Azul Pinochet-Barros, Lance C Seefeldt, Betül Kaçar   +6 more
doaj   +2 more sources

Classifying the metal dependence of uncharacterized nitrogenases [PDF]

Frontiers in Microbiology, 2013
Nitrogenase enzymes have evolved complex iron-sulfur (Fe-S) containing cofactors that most commonly contain molybdenum (MoFe, Nif) as a heterometal but also exist as vanadium (VFe, Vnf) and heterometal independent (Fe-only, Anf) forms.
Shawn E Mcglynn, Eric S Boyd, John W. Peters, Victoria J Orphan   +3 more
doaj   +4 more sources

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, Yvonne Pfänder, Sina Schäkermann, Julia Elisabeth Bandow, Bernd Masepohl   +4 more
doaj   +2 more sources

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, B. Hoffman, J. Peters, S. Raugei, D. Beratan, E. Antony, D. Dean   +6 more
semanticscholar   +4 more sources

Genetic analysis of the NifM dependence of the nitrogenase iron proteins [PDF]

mBio
NifH maturation in certain diazotrophic bacteria depends on NifM, a protein with a PpiC-isomerase domain. Intriguingly, the putative proline substrate for NifM is present in NifH proteins from strains lacking nifM, raising questions regarding the actual ...
Zhuoting Xie, Shuyi Cai, Haoyang Chen, Shuyuan Kong, Letian Tang, Yi-Ping Wang, Jianguo Yang   +6 more
doaj   +2 more sources

Accessory Proteins of the Nitrogenase Assembly, NifW, NifX/NafY, and NifZ, Are Essential for Diazotrophic Growth in the Nonheterocystous Cyanobacterium Leptolyngbya boryana

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, Haruki Yamamoto, Narumi Kamiya, Hiroya Kotani, Hisanori Yamakawa, Ryoma Tsujimoto, Yuichi Fujita, Yuichi Fujita   +7 more
doaj   +2 more sources

Structural basis for the conformational protection of nitrogenase from O2 [PDF]

Structural Dynamics
The low reduction potentials required for the reduction of dinitrogen (N2) render metal-based nitrogen-fixation catalysts vulnerable to irreversible damage by dioxygen (O2).
Sarah M Narehood, Brian D Cook, Suppachai Srisantitham, Vanessa Eng, Angela A Shiau, Kelly L McGuire, R. David Britt, Mark A Herzik, F. Akif Tezcan   +8 more
doaj   +2 more sources

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

Nature Chemistry, 2019
The electronic structure of the nitrogenase metal cofactors is central to nitrogen fixation. However, the P-cluster and iron molybdenum cofactor, each containing eight irons, have resisted detailed characterization of their electronic properties. Through
Chan, Garnet Kin-Lic, Guo, Sheng, Li, Zhendong, Sun, Qiming   +3 more
core   +4 more sources