Zobrazeno 1 - 10
of 325
pro vyhledávání: '"Edward A. Berry"'
Publikováno v:
Cellular and Molecular Life Sciences. 76:4023-4042
Succinate dehydrogenase (SDH) also known as complex II or succinate:quinone oxidoreductase is an enzyme involved in both oxidative phosphorylation and tricarboxylic acid cycle; the processes that generate energy. SDH is a multi-subunit enzyme which r
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 22
International journal of molecular sciences
21 (2020): 1–12. doi:10.3390/ijms21228521
info:cnr-pdr/source/autori:Forte, Elena; Giuffrè, Alessandro; Huang, Li Shar; Berry, Edward A.; Borisov, Vitaliy B./titolo:Nitric oxide does not inhibit but is metabolized by the cytochrome bcc-aa3<%2Finf> supercomplex/doi:10.3390%2Fijms21228521/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:1/pagina_a:12/intervallo_pagine:1–12/volume:21
Volume 21
Issue 22
International journal of molecular sciences
21 (2020): 1–12. doi:10.3390/ijms21228521
info:cnr-pdr/source/autori:Forte, Elena; Giuffrè, Alessandro; Huang, Li Shar; Berry, Edward A.; Borisov, Vitaliy B./titolo:Nitric oxide does not inhibit but is metabolized by the cytochrome bcc-aa3<%2Finf> supercomplex/doi:10.3390%2Fijms21228521/rivista:International journal of molecular sciences (Print)/anno:2020/pagina_da:1/pagina_a:12/intervallo_pagine:1–12/volume:21
Nitric oxide (NO) is a well-known active site ligand and inhibitor of respiratory terminal oxidases. Here, we investigated the interaction of NO with a purified chimeric bcc-aa3 supercomplex composed of Mycobacterium tuberculosis cytochrome bcc and M
Publikováno v:
International Journal of Molecular Sciences
Nitric oxide (NO) is a well-known active site ligand and inhibitor of respiratory terminal oxidases. Here, we investigated the interaction of NO with a purified chimeric bcc-aa3 supercomplex composed of Mycobacterium tuberculosis cytochrome bcc and M
Publikováno v:
The EMBO Journal. 35:1694-1706
Vacuolar ATPases (V‐ATPases) are essential proton pumps that acidify the lumen of subcellular organelles in all eukaryotic cells and the extracellular space in some tissues. V‐ATPase activity is regulated by a unique mechanism referred to as reve
Autor:
Edward A. Berry, Gil-Ja Jhon, Dong Hae Shin, Jimin Park, Jooyoung Lee, Mi-Sun Kim, Keehyung Joo
Publikováno v:
Molecules and Cells
We have solved the crystal structure of a predicted fructose-specific enzyme IIB(fruc) from Escherichia coli (EcEIIB(fruc)) involved in the phosphoenolpyruvate-carbohydrate phosphotransferase system transferring carbohydrates across the cytoplasmic m
Autor:
Kevin Pethe, Edward A. Berry, Jichan Jang, Mi-Sun Kim, Li-Shar Huang, Nurlilah Binte Ab Rahman
Publikováno v:
The Journal of Biological Chemistry
Background: Mycobacteria have no soluble cytochrome c; the electron transfer chain involves a Complex III-IV “supercomplex.” Results: Expression of the M. tuberculosis Complex III in M. smegmatis lacking native complex yields a functional hybrid
Publikováno v:
The Journal of Membrane Biology. 247:981-996
Detergents classically are used to keep membrane proteins soluble in aqueous solutions, but they tend to destabilize them. This problem can be largely alleviated thanks to the use of amphipols (APols), small amphipathic polymers designed to substitut
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827(11-12):1258-1277
X-ray crystal structures of bc1 complexes obtained over the last 15 years have provided a firm structural basis for our understanding of the complex. For the most part there is good agreement between structures from different species, different cryst
Publikováno v:
Archives of biochemistry and biophysics. 604
Mitochondrial Complex II (Succinate: ubiquinone oxidoreductase) has a covalently bound FAD cofactor in its largest subunit (SDHA), which accepts electrons from oxidation of succinate during catalysis. The mechanism of flavin attachment, and factors i
Autor:
Edward A. Berry, Li-Shar Huang
Publikováno v:
Advances in Photosynthesis and Respiration ISBN: 9789401774796
A detailed description is provided of the different positions observed for the Rieske iron-sulfur protein in different crystal structures of the bc 1 complex, and the conformational changes taking place in the “neck” or “linker” region to mak
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15c9fc1069e1ea7d82bb50428be73e49
https://doi.org/10.1007/978-94-017-7481-9_11
https://doi.org/10.1007/978-94-017-7481-9_11