Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Vitaliy B. Borisov"'
Publikováno v:
Antioxidants, Vol 10, Iss 6, p 839 (2021)
Reactive oxygen species (ROS) comprise the superoxide anion (O2•−), hydrogen peroxide (H2O2), hydroxyl radical (•OH), and singlet oxygen (1O2). ROS can damage a variety of macromolecules, including DNA, RNA, proteins, and lipids, and compromise
Externí odkaz:
https://doaj.org/article/65802faf26e1498cbea4ff45536f4a9f
Publikováno v:
Antioxidants, Vol 10, Iss 1, p 13 (2020)
Interaction of two redox enzymes of Escherichia coli, cytochrome bo3 and cytochrome bd-I, with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution respirometry and absorption spectroscopy. At pH 7.0, the oxygen reductase acti
Externí odkaz:
https://doaj.org/article/c2d469722a884427be11ae152526387b
Autor:
Elena Forte, Vitaliy B. Borisov, Albert Davletshin, Daniela Mastronicola, Paolo Sarti, Alessandro Giuffrè
Publikováno v:
mBio, Vol 4, Iss 6 (2013)
Externí odkaz:
https://doaj.org/article/d9c2e151163940389a91b61dba0aafa6
Publikováno v:
PLoS ONE, Vol 11, Iss 5, p e0155186 (2016)
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-dependent respiratory chain of Escherichia coli. It contains one low-spin haem (b558) and the two high-spin haems (b595 and d) as the redox-active cofactors.
Externí odkaz:
https://doaj.org/article/a9e8c86ee7214f509370e1d7da324458
Publikováno v:
International journal of molecular sciences. 23(6)
Cytochrome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::181b84c012f5fa02b1d9ab76a4f2e07c
https://pubmed.ncbi.nlm.nih.gov/35328590
https://pubmed.ncbi.nlm.nih.gov/35328590
Cytochrome bd-II is one of the three terminal quinol oxidases of the aerobic respiratory chain of Escherichia coli. Preparations of the detergent-solubilized untagged bd-II oxidase isolated from the bacterium were shown to scavenge hydrogen peroxide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ed44105467393427145fb3fa41ead22
https://hdl.handle.net/11573/1633615
https://hdl.handle.net/11573/1633615
Autor:
Natalia V. Azarkina, Vitaliy B. Borisov, Ilya P. Oleynikov, Roman V. Sudakov, Tatiana V. Vygodina
Publikováno v:
International Journal of Molecular Sciences. 24:6428
The review focuses on recent advances regarding the effects of natural and artificial amphipathic compounds on terminal oxidases. Terminal oxidases are fascinating biomolecular devices which couple the oxidation of respiratory substrates with generat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7704373377cbb8ecfa94b3f7fe27f26
https://doi.org/10.3390/ijms24076428
https://doi.org/10.3390/ijms24076428
Publikováno v:
International Journal of Molecular Sciences. 24:5417
F1·Fo-ATP synthases/ATPases (F1·Fo) are molecular machines that couple either ATP synthesis from ADP and phosphate or ATP hydrolysis to the consumption or production of a transmembrane electrochemical gradient of protons. Currently, in view of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcf30cf0a1d45b6af03708aee5163dfe
https://doi.org/10.3390/ijms24065417
https://doi.org/10.3390/ijms24065417
Publikováno v:
Antioxidants, Vol 10, Iss 13, p 13 (2021)
Antioxidants
Volume 10
Issue 1
Antioxidants
Volume 10
Issue 1
Interaction of two redox enzymes of Escherichia coli, cytochrome bo3 and cytochrome bd-I, with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution respirometry and absorption spectroscopy. At pH 7.0, the oxygen reductase acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91a7a5d7b346e647fca2fe1bf840019e
https://www.mdpi.com/2076-3921/10/1/13
https://www.mdpi.com/2076-3921/10/1/13
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e95617 (2014)
Cytochrome bd is a tri-heme (b558, b595, d) respiratory oxygen reductase that is found in many bacteria including pathogenic species. It couples the electron transfer from quinol to O2 with generation of an electrochemical proton gradient. We examine
Externí odkaz:
https://doaj.org/article/edf3ced1be974002ae10a29886b89f4b