Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Marian Fabian"'
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 20, p 12580 (2022)
The reduction of O2 in respiratory cytochrome c oxidases (CcO) is associated with the generation of the transmembrane proton gradient by two mechanisms. In one of them, the proton pumping, two different types of the ferryl intermediates of the cataly
Externí odkaz:
https://doaj.org/article/c8eab599af094c34916b8952e2a6312a
Autor:
MarCia T Ekworomadu, Catherine B Poor, Cedric P Owens, Miriam A Balderas, Marian Fabian, John S Olson, Frank Murphy, Erol Bakkalbasi, Erin S Honsa, Chuan He, Celia W Goulding, Anthony W Maresso
Publikováno v:
PLoS Pathogens, Vol 8, Iss 3, p e1002559 (2012)
To replicate in mammalian hosts, bacterial pathogens must acquire iron. The majority of iron is coordinated to the protoporphyrin ring of heme, which is further bound to hemoglobin. Pathogenic bacteria utilize secreted hemophores to acquire heme from
Externí odkaz:
https://doaj.org/article/56c677eeda1c4146833e8d2069b9ff28
Publikováno v:
Biochemistry. Biokhimiia. 86(1)
Several ferryl states of the catalytic heme a3-CuB center of the respiratory cytochrome c oxidases (CcOs) are observed during the reduction of O2 to H2O. One of the P-type ferryl forms, PM, is produced by the reaction of the two-electron reduced CcO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e683209f7cc660f5d7a1ea39e74973a6
https://pubmed.ncbi.nlm.nih.gov/33705283
https://pubmed.ncbi.nlm.nih.gov/33705283
Autor:
Ludmila Mikulova, Erik Cizmar, Marian Fabian, Daniel Jancura, Katarina Kopcova, Tereza Sztachova, Ivana Pechova
Publikováno v:
Biochimica et biophysica acta. Bioenergetics. 1861(9)
Cytochrome a was suggested as the key redox center in the proton pumping process of bovine cytochrome c oxidase (CcO). Recent studies showed that both the structure of heme a and its immediate vicinity are sensitive to the ligation and the redox stat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6548c717111dfe5666da5f58babf2e9a
https://pubmed.ncbi.nlm.nih.gov/32485159
https://pubmed.ncbi.nlm.nih.gov/32485159
Publikováno v:
Biochemistry. 57:4105-4113
Second-derivative absorption spectroscopy was employed to monitor the response of effective symmetry of cytochromes a and a3 to the redox and ligation states of bovine cytochrome c oxidase (CcO). The Soret band π → π* electronic transitions were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::811a5d3b5df7d3f1030ce590867f63ff
https://doi.org/10.1021/acs.biochem.8b00459
https://doi.org/10.1021/acs.biochem.8b00459
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1862:148447
During catalysis of cytochrome c oxidases (CcO) several ferryl intermediates of the catalytic heme a3-CuB center are observed. In the PM ferryl state, produced by the reaction of two-electron reduced CcO with O2, the ferryl iron of heme a3 and a free
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b903ca3e736cc26cf769f3c10d076bf7
https://doi.org/10.1016/j.bbabio.2021.148447
https://doi.org/10.1016/j.bbabio.2021.148447
Publikováno v:
Biochemistry
In the absence of external electron donors, oxidized bovine cytochrome c oxidase (CcO) exhibits the ability to decompose excess H2O2. Depending on the concentration of peroxide, two mechanisms of degradation were identified. At submillimolar peroxide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37014c1bc5278fc5f2591b225443220b
https://doi.org/10.1021/bi401078b
https://doi.org/10.1021/bi401078b
Autor:
Qilin Li, Wenxiu Que, Jonathon Brame, Yulong Liao, Marian Fabian, Pedro J. J. Alvarez, Zongming Xiu, Haixia Xie
Publikováno v:
Journal of Hazardous Materials. 260:434-441
This study investigates the photocatalytic efficiency, type of reactive oxygen species (ROS) produced, and potential for structural and morphological modification of anodic TiO 2 nanotubes (NTs) synthesized using a novel, energy efficient, low temper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d341e800aa275e150889663db945886
https://doi.org/10.1016/j.jhazmat.2013.05.047
https://doi.org/10.1016/j.jhazmat.2013.05.047
Publikováno v:
Journal of Biological Chemistry. 286:33652-33660
Pathogenic bacteria require iron to replicate inside mammalian hosts. Recent studies indicate that heme acquisition in Gram-positive bacteria is mediated by proteins containing one or more near-iron transporter (NEAT) domains. Bacillus anthracis is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70340bbcecb393f33166f884f92c9ca6
https://doi.org/10.1074/jbc.m111.241687
https://doi.org/10.1074/jbc.m111.241687
Publikováno v:
Free Radical Biology and Medicine. 49:1574-1581
An excess of ferricytochrome c protects purified mitochondrial cytochrome c oxidase and bound cardiolipin from hydrogen peroxide-induced oxidative modification. All of the peroxide-induced changes within cytochrome c oxidase, such as oxidation of Trp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03d66b00593a5d3fa1ffcac371c1888c
https://doi.org/10.1016/j.freeradbiomed.2010.08.019
https://doi.org/10.1016/j.freeradbiomed.2010.08.019