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pro vyhledávání: '"cytochrome c nitrite reductase"'
Akademický článek
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Autor:
Matthew Tracy, Julius Campeciño, Victor Sosa Alfaro, Sean Elliott, Nicolai Lehnert, Eric L. Hegg
Publikováno v:
Biochemistry. 60:1853-1867
Cytochrome c nitrite reductases (CcNIR or NrfA) play important roles in the global nitrogen cycle by conserving the usable nitrogen in the soil. Here, the electron storage and distribution properties within the pentaheme scaffold of Geobacter lovleyi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::297f4c9d898cda191842ab91a089a4ec
https://doi.org/10.1021/acs.biochem.0c00977
https://doi.org/10.1021/acs.biochem.0c00977
Autor:
Quentin C Durfee, Demet Kekilli, Kelsey J Robinson, Colin R. Andrew, Michael A. Hough, Brianna N Brown
Publikováno v:
Inorganic Chemistry. 59:14162-14170
Hydroxylamine (NH2OH or HA) is a redox-active nitrogen oxide that occurs as a toxic intermediate in the oxidation of ammonium by nitrifying and methanotrophic bacteria. Within ammonium containing environments, HA is generated by ammonia monooxygenase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::99c59d11b013c6bbffc2b5b5a03cf448
https://doi.org/10.1021/acs.inorgchem.0c01925
https://doi.org/10.1021/acs.inorgchem.0c01925
Autor:
Marius Schmidt, Natalia Stein, Yingxi Mao, A. Andrew Pacheco, Shahid Shahid, Brian Bennett, Mahbbat Ali
Publikováno v:
Journal of the American Chemical Society. 141:13358-13371
Cytochrome c nitrite reductase (ccNiR) is a periplasmic, decaheme homodimeric enzyme that catalyzes the six-electron reduction of nitrite to ammonia. Under standard assay conditions catalysis proceeds without detected intermediates, and it has been a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab9e704ed43d6d97db205d8946f6df71
https://doi.org/10.1021/jacs.9b03036
https://doi.org/10.1021/jacs.9b03036
Autor:
A. Andrew Pacheco, Shahid Shahid
Publikováno v:
The FASEB Journal. 35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e127befa3f6d0effd68e699a8b000c07
https://doi.org/10.1096/fasebj.2021.35.s1.00441
https://doi.org/10.1096/fasebj.2021.35.s1.00441
Autor:
Monteiro, Tiago Carvalho
The present thesis focuses on the application of two distinct enzymes – cytochrome c nitrite reductase (ccNiR) and paraoxonase 1 (PON1) – as the key elements in the development of two electrochemical analytical devices, namely a 3rd generation mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1437::c0719dc15db20aad22cb4601c7337014
https://hdl.handle.net/10362/113413
https://hdl.handle.net/10362/113413
Autor:
Satyanarayana Lagishetty, Zdzislaw Wawrzak, Julius Campeciño, Victor Sosa Alfaro, Eric L. Hegg, Gemma Reguera, Nicolai Lehnert, Jian Hu
Publikováno v:
J Biol Chem
Cytochrome c nitrite reductase (NrfA) catalyzes the reduction of nitrite to ammonium in the dissimilatory nitrate reduction to ammonium (DNRA) pathway, a process that competes with denitrification, conserves nitrogen, and minimizes nutrient loss in s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f98791c1c9c15ffb3afb7ce2c276169
https://europepmc.org/articles/PMC7450111/
https://europepmc.org/articles/PMC7450111/
Publikováno v:
Journal of the American Chemical Society. 140:16888-16892
A cobalt-tripeptide complex (CoGGH) is developed as an electrocatalyst for the selective six-electron, eight-proton reduction of nitrite to ammonium in aqueous buffer near neutral pH. The onset potential for nitrite reduction occurs at -0.65 V vs Ag/
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99f8a0741e0deee2228af51418bd2e80
https://doi.org/10.1021/jacs.8b09612
https://doi.org/10.1021/jacs.8b09612
Autor:
Konstantin M. Boyko, M. V. Kovalchuk, Yu. M. Chesnokov, A.V. Lipkin, Alexander G. Myasnikov, Evgeny Pichkur, Timur Baymukhametov, Vladimir Popov, Tamara V. Tikhonova, A. L. Vasiliev
Publikováno v:
Acta Naturae. 10:48-56
The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5dafa3cddd7b799e63ffa83c15d5522f
https://doi.org/10.32607/20758251-2018-10-3-48-56
https://doi.org/10.32607/20758251-2018-10-3-48-56
Autor:
Yasuhiro Arikawa, Yuji Otsubo, Shinnosuke Horiuchi, Keisuke Umakoshi, Hiroki Fujino, Eri Sakuda
Publikováno v:
Journal of the American Chemical Society. 140:842-847
The fundamental biogeochemical cycle of nitrogen includes cytochrome c nitrite reductase, which catalyzes the reduction of nitrite ions to ammonium with eight protons and six electrons (NO2– + 8H+ + 6e– → NH4+ + 2H2O). This reaction has motivat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9ef7f0fe2004ac79a4b206682e3364c
https://doi.org/10.1021/jacs.7b12020
https://doi.org/10.1021/jacs.7b12020