Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Mackenzie J. Field"'
Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster
Publikováno v:
J Am Chem Soc
Nitrogenase catalyzes the multi-electron reduction of dinitrogen to ammonia. Electron transfer in the catalytic protein (MoFeP) proceeds through a unique [8Fe-7S] cluster (P-cluster) to the active site (FeMoco). In the reduced, all-ferrous (PN) state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c1d5f6b659f6375daa7a6938f640b3a
https://doi.org/10.1021/jacs.2c09480
https://doi.org/10.1021/jacs.2c09480
Publikováno v:
Journal of the American Chemical Society. 144:19272-19283
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e8681f646e28c3b1f7a21827d2c351a
https://doi.org/10.1021/jacs.2c05459
https://doi.org/10.1021/jacs.2c05459
Publikováno v:
Journal of the American Chemical Society, vol 143, iss 34
Nonheme iron oxygenases utilize dioxygen to accomplish challenging chemical oxidations. A further understanding of the Fe-O2 intermediates implicated in these processes is challenged by their highly transient nature. To that end, we have developed a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b02d45f221c1ee121c8de71f662f5aaf
https://doi.org/10.1021/jacs.1c05276
https://doi.org/10.1021/jacs.1c05276
Non-heme iron oxygenases utilize dioxygen to accomplish challenging chemical oxidations. Further understanding of the Fe-O2 intermediates implicated in these processes is challenged by their highly transient nature. To that end, we have developed a l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::577080d099c92276b9be6b905a226b11
https://doi.org/10.26434/chemrxiv.14681229
https://doi.org/10.26434/chemrxiv.14681229
Autor:
Mackenzie J. Field, Noreen E. Gentry, Anna C. Brezny, Jennifer L. Peper, Michael Green, James M. Mayer
Publikováno v:
J Phys Chem C Nanomater Interfaces
Electrons added to TiO(2) and other semiconductors often occupy trap states, whose reactivity can determine the catalytic and stoichiometric chemistry of the material. We previously showed that reduced aqueous colloidal TiO(2) nanoparticles have two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6ae84e18a09ee23c28bef9945271a88
https://europepmc.org/articles/PMC8232823/
https://europepmc.org/articles/PMC8232823/
Publikováno v:
Nature chemistry
Nature chemistry, vol 11, iss 5
Nature chemistry, vol 11, iss 5
The bottom-up design and construction of functional metalloproteins remains a formidable task in biomolecular design. While numerous strategies have been used to create new metalloproteins, preexisting knowledge of the tertiary and quaternary protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3812d921c6fc7a51a3414b6bb124102e
https://pubmed.ncbi.nlm.nih.gov/30886429
https://pubmed.ncbi.nlm.nih.gov/30886429
Publikováno v:
Physical Chemistry Chemical Physics. 18:30907-30911
Selective functionalization of unactivated C–H bonds is an ongoing chemical challenge. C–H activation requires the transfer of H+ and e−, so called proton-coupled electron transfer (PCET) reactions. Recent efforts in photochemical PCET involvin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96a26a373b73016b23c6e3bddafd0114
https://doi.org/10.1039/c6cp06418c
https://doi.org/10.1039/c6cp06418c
Using an artificial tryptophan 'wire' in cytochrome c peroxidase for oxidation of organic substrates
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 46(33)
Lignolytic peroxidases use an electron transfer (ET) pathway that involves amino acid-mediated substrate oxidation at the surface of the protein rather than at an embedded heme site. In many of these peroxidases, redox catalysis takes place at a subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7592e3e395e135b781aeb3af1e287e5
https://pubmed.ncbi.nlm.nih.gov/28792039
https://pubmed.ncbi.nlm.nih.gov/28792039