Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Dimitri, Niks"'
Autor:
Joel E. Graham, Dimitri Niks, Grant M. Zane, Qin Gui, Kellie Hom, Russ Hille, Judy D. Wall, C. S. Raman
Publikováno v:
ACS Catalysis. 12:10449-10471
The reversible two-electron interconversion of formate and CO2 is catalyzed by both non-metallo and metallo-formate dehydrogenases (FDHs). The latter group comprises molybdenum-or tungsten-containing enzymes with the metal coordinated by two equivale
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c833194f2e37201d38ccafa3902aadfd
https://doi.org/10.1021/acscatal.2c00316
https://doi.org/10.1021/acscatal.2c00316
Publikováno v:
Methods in Enzymology ISBN: 9780443152764
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2561313030de091f9f48fe15fbca4c2d
https://doi.org/10.1016/bs.mie.2023.03.011
https://doi.org/10.1016/bs.mie.2023.03.011
Autor:
Russ Hille, Tynan Young, Dimitri Niks, Sheron Hakopian, Timothy K. Tam, Xuejun Yu, Ashok Mulchandani, Gregor M. Blaha
Publikováno v:
Inorganics, Vol 8, Iss 7, p 41 (2020)
Here, we report recent progress our laboratories have made in understanding the maturation and reaction mechanism of the cytosolic and NAD+-dependent formate dehydrogenase from Cupriavidus necator. Our recent work has established that the enzyme is f
Externí odkaz:
https://doaj.org/article/422c3031eda84ac7b896a0d07c62e7bb
Autor:
Yuliana K. Bosken, Huanbin Zhou, Li Fan, Chia-en A. Chang, Wenbo Ma, Leonard J. Mueller, Shih-Hsin Kan, Rittik K. Ghosh, Eduardo Hilario, Michael F. Dunn, Dimitri Niks, Rizi Ai
Publikováno v:
Protein Sci
Antibiotic and antimicrobial resistance is a continually growing challenge in the treatment of various bacterial infections worldwide. New drugs and new drug targets are necessary to curb the threat of infectious diseases caused by multidrug-resistan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2ab6b00a07ca389633351a96410ff9e
https://doi.org/10.1002/pro.4236
https://doi.org/10.1002/pro.4236
Publikováno v:
Journal of Biological Chemistry. :104853
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb0b2d80e00ec1ed95920f287aa137ff
https://doi.org/10.1016/j.jbc.2023.104853
https://doi.org/10.1016/j.jbc.2023.104853
The nature of air-inactivation of the formate dehydrogenase FdsDABG from Cupriavidus necator has been investigated. It is found that superoxide, generated in the reaction of reduced enzyme with oxygen, is responsible for the loss of activity and that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c820009e46510a64846d495d7934d87
https://escholarship.org/uc/item/5hg9r543
https://escholarship.org/uc/item/5hg9r543
Autor:
Russ, Hille, Dimitri, Niks
Publikováno v:
Methods in enzymology. 666
A description is provided of the contributions made to our understanding of molybdenum-containing enzymes through the application of electron paramagnetic resonance spectroscopy and related methods, by way of illustrating how these can be applied to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::54e16c0eea169fcc7fd2edb90ff60883
https://pubmed.ncbi.nlm.nih.gov/35465925
https://pubmed.ncbi.nlm.nih.gov/35465925
Autor:
Wayne, Vigil, Jessica, Tran, Dimitri, Niks, Gerrit J, Schut, Xiaoxuan, Ge, Michael W W, Adams, Russ, Hille
Publikováno v:
The Journal of biological chemistry. 298(6)
The EtfAB components of two bifurcating flavoprotein systems, the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from the bacterium Megasphaera elsdenii and the menaquinone-dependent NADH:ferredoxin oxidoreductase from the archaeon Pyrobaculum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::950f47abcc08eb0763d83ffebd617f45
https://pubmed.ncbi.nlm.nih.gov/35429498
https://pubmed.ncbi.nlm.nih.gov/35429498
Autor:
Russ Hille, Dimitri Niks
Publikováno v:
Methods in Enzymology ISBN: 9780323999748
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39cb8583f103a5fe56c2944f074353ae
https://doi.org/10.1016/bs.mie.2022.02.006
https://doi.org/10.1016/bs.mie.2022.02.006
Autor:
Viktoriia Liu, Leonard J. Mueller, Yangyang Wang, Michael F. Dunn, Jacob B. Holmes, Eduardo Hilario, Varun V. Sakhrani, Rittik K. Ghosh, Dimitri Niks
Publikováno v:
Biochemistry
The tryptophan synthase (TS) bienzyme complexes found in bacteria, yeasts, and molds are pyridoxal 5'-phosphate (PLP)-requiring enzymes that synthesize l-Trp. In the TS catalytic cycle, switching between the open and closed states of the α- and β-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::820c9a9c40d126d7e982381d080bb3a4
https://pubmed.ncbi.nlm.nih.gov/34595921
https://pubmed.ncbi.nlm.nih.gov/34595921