Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Marta S. P. Carepo"'
Autor:
Vitor H. Mordido, Marta S. P. Carepo, Cristina M. Cordas, Navendu Paul, Jörg Simon, Isabel Moura, Sofia R. Pauleta
Publikováno v:
Frontiers in Chemical Biology, Vol 3 (2024)
Cytochrome c552 from Wolinella succinogenes is one of the few examples of a low reduction potential class I c-type cytochrome with a mixture of high/low spin state populations observed in its visible spectrum. Analysis of its structural model suggest
Externí odkaz:
https://doaj.org/article/2db081c833914966aeaa6863dc646b43
Autor:
Rafael A. Baraúna, Agenor V. Santos, Diego A. Graças, Daniel M. Santos, Rubens Ghilardi Júnior, Adriano M. C. Pimenta, Marta S. P. Carepo, Maria P.C. Schneider, Artur Silva
Publikováno v:
Genetics and Molecular Biology, Vol 38, Iss 2, Pp 227-230 (2015)
Several studies of the physiological responses of different organisms exposed to extremely low-frequency electromagnetic fields (ELF-EMF) have been described. In this work, we report the minimal effects of in situ exposure to ELF-EMF on the global pr
Externí odkaz:
https://doaj.org/article/a944a0e52d9f4bf3a20a72fc2825a86c
Autor:
Pedro M S, Bragança, Marta S P, Carepo, Sofia R, Pauleta, Tyler B J, Pinter, Maddalena, Elia, Cristina M, Cordas, Isabel, Moura, Vincent L, Pecoraro, José J G, Moura
Publikováno v:
Journal of inorganic biochemistry. 240
The rational design and functionalization of small, simple, and stable peptides scaffolds is an attractive avenue to mimic catalytic metal-centres of complex proteins, relevant for the design of metalloenzymes with environmental, biotechnological and
Publikováno v:
Coordination Chemistry Reviews. 387:436-449
Nitrous oxide is a potent greenhouse gas with a global warming impact 300-fold higher than carbon dioxide. Due to its exponential increase in the atmosphere and its implications in climate change there is the need to develop strategies to mitigate it
Publikováno v:
Journal of Photochemistry and Photobiology A: Chemistry. 372:59-62
Fluorescence spectroscopy is a powerful tool to comprehend macromolecules interaction. The characteristics of the fluorophore as well its behavior under the experimental conditions are central to ascertain the results. The present work characterizes
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Nitrous oxide reductase catalyzes the reduction of nitrous oxide (N2O) to dinitrogen (N2) and water at a catalytic tetranuclear copper sulfide center, named CuZ, overcoming the high activation energy of this reaction. In this center each Cu atom is c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::b1e93727ba006efa7966926c8951a782
Nitrous oxide reductase catalyzes the reduction of nitrous oxide (N2O) to dinitrogen (N2) and water at a catalytic tetranuclear copper sulfide center, named CuZ, overcoming the high activation energy of this reaction. In this center each Cu atom is c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::155b2de494dad41d6e0fe6cd1e0bb47d
https://doi.org/10.1515/9783110589757-011
https://doi.org/10.1515/9783110589757-011
Autor:
Luiz Gonzaga de França Lopes, Marta S. P. Carepo, Pedro Mikael da Silva Costa, Marie Alda Gilles-Gonzalez, Wellinson G. Guimarães, Eduardo H.S. Sousa, Ana C. S. Gondim
Publikováno v:
Journal of Inorganic Biochemistry. 172:129-137
FixL from Rhizobium etli (ReFixL) is a hybrid oxygen sensor protein. Signal transduction in Re FixL is effected by a switch off of the kinase activity on binding of an oxygen molecule to ferrous heme iron in another domain. Cyanide can also inhibit t
Autor:
Eduardo H.S. Sousa, Izaura C.N. Diógenes, Marta S. P. Carepo, Paul V. Bernhardt, Tércio de F. Paulo, Nathalie Honorio-Felício, Luiz Gonzaga de França Lopes
Publikováno v:
Journal of Inorganic Biochemistry. 164:34-41
Conformational changes associated to sensing mechanisms of heme-based protein sensors are a key molecular event that seems to modulate not only the protein activity but also the potential of the Fe III/II redox couple of the heme domain. In this work
Autor:
Alejandro K. Samhan-Arias, Marta S. P. Carepo, José J. G. Moura, Isabel Moura, Luisa B. Maia, Cristina M. Cordas, Carlos Gutiérrez-Merino
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
FCT/MCTES (UID/QUI/50006/2019) FCT/MCTES post-doctoral grant (SFRH/BPD/100069/2014) Recently, we observed that at extreme alkaline pH, cytochrome b 5 (Cb 5 ) acquires a peroxidase-like activity upon formation of a low spin hemichrome associated with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3beb878f5496c9a773dfbf182d0e0835
http://www.scopus.com/inward/record.url?scp=85062720207&partnerID=8YFLogxK
http://www.scopus.com/inward/record.url?scp=85062720207&partnerID=8YFLogxK