Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Marco Allegrozzi"'
Autor:
Sven Christian Feifel, Kai Ralf Stieger, Andreas Kapp, Dennis Weber, Marco Allegrozzi, Mario Piccioli, Paola Turano, Fred Lisdat
Publikováno v:
ACS Omega, Vol 1, Iss 6, Pp 1058-1066 (2016)
Externí odkaz:
https://doaj.org/article/00235913a1ed47fabb5f298c041fe90d
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 6, p 2134 (2020)
It is well known that axial coordination of heme iron in mitochondrial cytochrome c has redox-dependent stability. The Met80 heme iron axial ligand in the ferric form of the protein is relatively labile and can be easily replaced by alternative amino
Externí odkaz:
https://doaj.org/article/213dc04814b34f73b695e4c588234c59
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 6, p 2134 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 6
International Journal of Molecular Sciences
Volume 21
Issue 6
It is well known that axial coordination of heme iron in mitochondrial cytochrome c has redox-dependent stability. The Met80 heme iron axial ligand in the ferric form of the protein is relatively labile and can be easily replaced by alternative amino
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 19:615-622
Integrated ferritin protein cage function is the reversible synthesis of protein-caged, solid Fe2O3·H2O minerals from Fe(2+) for metabolic iron concentrates and oxidant protection; biomineral order differs in different ferritin proteins. The conserv
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry
This study summarizes results which have been obtained by a mutational study of human cytochrome c. The protein can be used as a recognition element in analytical assays and biosensors for superoxide radicals since ferricytochrome c reacts with super
Autor:
Kai Ralf Stieger, Mario Piccioli, Paola Turano, Dennis Weber, Sven Christian Feifel, Andreas Kapp, Fred Lisdat, Marco Allegrozzi
Publikováno v:
ACS Omega, Vol 1, Iss 6, Pp 1058-1066 (2016)
The redox behavior of proteins plays a crucial part in the design of bioelectronic systems. We have demonstrated several functional systems exploiting the electron exchange properties of the redox protein cytochrome c (cyt c) in combination with enzy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be22578ae3ff4a0f472a558cccb9712c
https://opus4.kobv.de/opus4-th-wildau/frontdoor/index/index/docId/675
https://opus4.kobv.de/opus4-th-wildau/frontdoor/index/index/docId/675
Autor:
Claudia Temperini, Anna Rita Bilia, Paola Turano, Francesca Piccioli, Luigi Messori, Marco Allegrozzi, Franco Francesco Vincieri
Publikováno v:
Inorganica Chimica Acta. 357:4602-4606
The mechanism of action of trioxane antimalarial drugs is still largely controversial and warrants further investigation. We report here on the direct reaction of artemisinin with hemin, carried out in DMSO, in the absence of reducing agents. The rea
Autor:
Claudio Luchinat, and Gaohua Liu, Ivano Bertini, Marco Allegrozzi, Yong Min Lee, Matthias B. L. Janik
Publikováno v:
Journal of the American Chemical Society. 122:4154-4161
A number of pseudocontact shifts (PCS) in monolanthanide-substituted Calbindin D9k (Ca2Cb hereafter), a protein of 75 amino acids, were measured for Ce(III), Yb(III), and Dy(III). The assignment of the shifts was obtained through the conventional ass
Publikováno v:
Langmuir : the ACS journal of surfaces and colloids. 27(7)
Here, we report on cytochrome c/bilirubin oxidase multilayer electrodes with different cytochrome c (cyt c) forms including mutant forms of human cyt c, which exhibit different reaction rates with bilirubin oxidase (BOD) in solution. The multilayer f
Publikováno v:
Analytical chemistry. 81(8)
The effect of introducing positive charges (lysines) in human cytochrome c (cyt c) on the redox properties and reaction rates of cyt c with superoxide radicals was studied. The mutated forms of this electron-transfer protein are used as sensorial rec