Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Simona Horsa"'
Publikováno v:
Journal of Photochemistry and Photobiology A: Chemistry. 221:84-89
Here we report the functionalization of a zeolite-like-metal organic framework of RHO topology with two cationic photosensitizers, methylene blue (MB + ) and phenosafranine (PS + ). The spectroscopic properties of encapsulated MB + are strongly influ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c4d73604d0b60463e262350be7591e9
https://doi.org/10.1016/j.jphotochem.2011.04.029
https://doi.org/10.1016/j.jphotochem.2011.04.029
Publikováno v:
Biochemistry. 47:11510-11517
Herein, we present photoacoustic calorimetry and transient absorption studies of the dynamics and energetics associated with dissociation of a ligand from Fe(2+) dehaloperoxidase (DHP) from Amphitrite ornata. Our data show that CO photodissociation i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c30bec185851a64e02ff0ed2eb32deee
https://doi.org/10.1021/bi8012033
https://doi.org/10.1021/bi8012033
Publikováno v:
Biophysical Journal. 98(3)
Chloroperoxidase (CPO) is the most versatile heme containing enzyme that exhibits peroxidase, catalase, halogenase and monooxigenase activities. The heme iron coordination resembles to P450s enzymes whereas the composition of the distal pocket is mor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04d119da8d8f9e591e7f3962e61ea90a
Publikováno v:
Biophysical Journal. 96(3)
Chloroperoxidase (CPO) is the most versatile heme peroxidase that can function as peroxidase, catalase, halogenase/dehalogenase and monooxigenase. The active site of CPO strongly resembles that of cytochrome P450 since the heme iron in both proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::647353e86f8a5a7942fdebee18ab8da7