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pro vyhledávání: '"Matthew Youngblut"'
Publikováno v:
Biochemistry. 51:10175-10185
Shewanella oneidensis cytochrome c nitrite reductase (soNrfA), a dimeric enzyme that houses five c-type hemes per protomer, carries out the six-electron reduction of nitrite and the two-electron reduction of hydroxylamine. Protein film voltammetry (P
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 13:1073-1083
Hydroxylamine oxidoreductase (HAO) from the ammonia-oxidizing bacterium Nitrosomonas europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is the second step in ammonia-dependent respiration. Here we show that, in
Autor:
Daniel T. Walters, A. Andrew Pacheco, Matthew Youngblut, Natalia Stein, Daniel J. Pauly, Brian Bennett, Graham R. Moran, John A. Conrad
Cytochrome c nitrite reductase (ccNiR) from Shewanella oneidensis, which catalyzes the six-electron reduction of nitrite to ammonia in vivo, was shown to oxidize hydroxylamine in the presence of large quantities of this substrate, yielding nitrite as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c26e8c5974560d13125eec384fcf409f
https://europepmc.org/articles/PMC5047060/
https://europepmc.org/articles/PMC5047060/
Autor:
Evan T. Judd, Tyler Goelzer, Marius Schmidt, Bilal H. Sayyed, Sean Elliott, Vukica Šrajer, Matthew Youngblut, A. Andrew Pacheco
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 17(4)
The high-yield expression and purification of Shewanella oneidensis cytochrome c nitrite reductase (ccNiR) and its characterization by a variety of methods, notably Laue crystallography, are reported. A key component of the expression system is an ar