Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Diana L. Wertz"'
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29270 (2012)
AOC3 is highly expressed in adipocytes and smooth muscle cells, but its function in these cells is currently unknown. The in vivo substrate(s) of AOC3 is/are also unknown, but could provide an invaluable clue to the enzyme's function. Expression of u
Externí odkaz:
https://doaj.org/article/bb121402748a4885b3c3d1ecb5046f83
Autor:
Lee-Loung Liou, Joan Selverstone Valentine, Edith Butler Gralla, Diana L. Wertz, Joy J. Goto, Thomas J. Lyons
Publikováno v:
Current Opinion in Chemical Biology. 2:253-262
The cellular biochemistry of dioxygen is Janus-faced. The good side includes numerous enzyme-catalyzed reactions of dioxygen that occur in respiration and normal metabolism, while the dark side encompasses deleterious reactions of species derived fro
Autor:
Raymond Y. N. Ho, Marlene F. Sisemore, Joan Selverstone Valentine, Diana L. Wertz, Matthias Selke
Publikováno v:
Journal of Molecular Catalysis A: Chemical. 117:71-82
Three different modes of oxygen activation by iron complexes are described: (1) Oxygen atom transfer by ferric porphyrin peroxo complexes to electron-deficient olefins via a nucleophilic mechanism, (2) oxidative dehydrogenation of a cyclam complex, p
Autor:
Judith P. Klinman, Diana L. Wertz
Publikováno v:
Handbook of Metalloproteins ISBN: 047086981X
Handbook of Metalloproteins
Handbook of Metalloproteins
Copper amine oxidases contain the covalently bound quinone cofactor, topaquinone, in addition to an active site copper. These proteins are widely distributed among both prokaryotes and eukaryotes and have been characterized with regard to kinetic and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79ae8226b5a88cf8c6cb7bb39a9be65d
https://doi.org/10.1002/0470028637.met192
https://doi.org/10.1002/0470028637.met192
Publikováno v:
Structure and Bonding ISBN: 9783540669432
For the past 20 years, cytochrome P450 researchers have sought to identify and to characterize the reactive intermediates in reactions of these enzymes. This review focuses on one of those postulated intermediates, the ferric heme peroxo complex, [(p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27aab71819e3493ea7a2e85d2541470e
https://doi.org/10.1007/3-540-46592-8_2
https://doi.org/10.1007/3-540-46592-8_2
Autor:
Matthias Selke, Diana L. Wertz, Joan Selverstone Valentine, Jennifer Driscoll, Marlene F. Sisemore
Publikováno v:
Journal of the American Chemical Society. 120:5331-5332