Zobrazeno 1 - 10
of 286
pro vyhledávání: '"Douglas C. Rees"'
Autor:
Rebeccah A. Warmack, Douglas C. Rees
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract Biological nitrogen fixation, performed by the enzyme nitrogenase, supplies nearly 50% of the bioavailable nitrogen pool on Earth, yet the structural nature of the enzyme intermediates involved in this cycle remains ambiguous. Here we presen
Externí odkaz:
https://doaj.org/article/ac48b35a775445708fca8e3d216a3ea5
Autor:
Lorenz Heidinger, Kathryn Perez, Thomas Spatzal, Oliver Einsle, Stefan Weber, Douglas C. Rees, Erik Schleicher
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Due to the complexity of the catalytic FeMo cofactor site in nitrogenases that mediates the reduction of molecular nitrogen to ammonium, mechanistic details of this reaction remain under debate. In this study, selenium- and sulfur-incorporat
Externí odkaz:
https://doaj.org/article/3533319ff4c04865b13a91688453b6fa
Autor:
Rebeccah A. Warmack, Ailiena O. Maggiolo, Andres Orta, Belinda B. Wenke, James B. Howard, Douglas C. Rees
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation that is essential for sustaining life. The active site FeMo-cofactor contains a [7Fe:1Mo:9S:1C] metallocluster coor
Externí odkaz:
https://doaj.org/article/be832672eab34ef78cf20fb18ca4bfdc
Autor:
Rebeccah A. Warmack, Douglas C. Rees
Publikováno v:
Molecules, Vol 28, Iss 24, p 7952 (2023)
Nitrogenases have the remarkable ability to catalyze the reduction of dinitrogen to ammonia under physiological conditions. How does this happen? The current view of the nitrogenase mechanism focuses on the role of hydrides, the binding of dinitrogen
Externí odkaz:
https://doaj.org/article/58e15f72c5334913baebbce306ae7337
Autor:
Aaron L Nichols, Zack Blumenfeld, Chengcheng Fan, Laura Luebbert, Annet EM Blom, Bruce N Cohen, Jonathan S Marvin, Philip M Borden, Charlene H Kim, Anand K Muthusamy, Amol V Shivange, Hailey J Knox, Hugo Rego Campello, Jonathan H Wang, Dennis A Dougherty, Loren L Looger, Timothy Gallagher, Douglas C Rees, Henry A Lester
Publikováno v:
eLife, Vol 11 (2022)
Externí odkaz:
https://doaj.org/article/098460172c5e405ebfd89ac4744a4398
Publikováno v:
eLife, Vol 11 (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 bi
Externí odkaz:
https://doaj.org/article/85234b48d7804c00a450ffc97fcb778f
Autor:
Chengcheng Fan, Douglas C Rees
Publikováno v:
eLife, Vol 11 (2022)
The ATP binding cassette (ABC) transporter of mitochondria (Atm) from Arabidopsis thaliana (AtAtm3) has been implicated in the maturation of cytosolic iron-sulfur proteins and heavy metal detoxification, plausibly by exporting glutathione derivatives
Externí odkaz:
https://doaj.org/article/1697e455bdbb4a5d95fc038613f1e3a7
Autor:
Aaron L Nichols, Zack Blumenfeld, Chengcheng Fan, Laura Luebbert, Annet EM Blom, Bruce N Cohen, Jonathan S Marvin, Philip M Borden, Charlene H Kim, Anand K Muthusamy, Amol V Shivange, Hailey J Knox, Hugo Rego Campello, Jonathan H Wang, Dennis A Dougherty, Loren L Looger, Timothy Gallagher, Douglas C Rees, Henry A Lester
Publikováno v:
eLife, Vol 11 (2022)
Nicotinic partial agonists provide an accepted aid for smoking cessation and thus contribute to decreasing tobacco-related disease. Improved drugs constitute a continued area of study. However, there remains no reductionist method to examine the cell
Externí odkaz:
https://doaj.org/article/4b4e86491b454335b0724b76381431a8
Autor:
Naima G Sharaf, Mona Shahgholi, Esther Kim, Jeffrey Y Lai, David G VanderVelde, Allen T Lee, Douglas C Rees
Publikováno v:
eLife, Vol 10 (2021)
NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-neg
Externí odkaz:
https://doaj.org/article/644cf02d64a6410194394509bed6ace7
Autor:
Stephanie D. Threatt, Douglas C. Rees
Publikováno v:
FEBS Letters. 597:45-58
Nitrogenase is the sole enzyme responsible for the ATP-dependent conversion of atmospheric dinitrogen into the bioavailable form of ammonia (NH₃), making this protein essential for the maintenance of the nitrogen cycle and thus life itself. Despite