Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Merche, Faro"'
Autor:
Achim Heinz, Rita Bernhardt, Isabel Nogués, Merche Faro, Milagros Medina, Carlos Gómez-Moreno, Burkhard Schiffler
Publikováno v:
European Journal of Biochemistry. 270:726-735
The opportunity to design enzymatic systems is becoming more feasible due to detailed knowledge of the structure of many proteins. As a first step, investigations have aimed to redesign already existing systems, so that they can perform a function di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::99668d7e03fb19676d617cda0a3145fe
https://doi.org/10.1046/j.1432-1033.2003.03433.x
https://doi.org/10.1046/j.1432-1033.2003.03433.x
Autor:
Susana Frago, Tomás Mayoral, Milagros Medina, Juan A. Hermoso, Carlos Gómez-Moreno, Julia Sanz-Aparicio, Merche Faro
Publikováno v:
European Journal of Biochemistry. 269:4938-4947
The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1eb5ea37aab9e92d31191d9df8684c16
https://doi.org/10.1046/j.1432-1033.2002.03194.x
https://doi.org/10.1046/j.1432-1033.2002.03194.x
Autor:
Milagros Medina, Tomás Mayoral, Carlos Gómez-Moreno, Julia Sanz-Aparicio, Merche Faro, Juan A. Hermoso
Publikováno v:
Journal of Molecular Biology. 319:1133-1142
The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c24d24efc056a67ee724fd821ae2430d
https://doi.org/10.1016/s0022-2836(02)00388-1
https://doi.org/10.1016/s0022-2836(02)00388-1
Publikováno v:
European Journal of Biochemistry. 269:2656-2661
Reduction potential determinations of K75E, E139K and E301A ferredoxin-NADP+ reductases provide valuable information concerning the factors that contribute to tune the flavin reduction potential. Thus, while E139 is not involved in such modulation, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d37828328d96060c8f25549325b8f707
https://doi.org/10.1046/j.1432-1033.2002.02925.x
https://doi.org/10.1046/j.1432-1033.2002.02925.x
Autor:
Julia Sanz-Aparicio, Tammy B. Brodie, Milagros Medina, Juan A. Hermoso, Marian T. Stankovich, Isabel Nogués, Tomás Mayoral, Merche Faro, Gordon Tollin, Carlos Gómez-Moreno, Marta Martínez-Júlvez, John K. Hurley
Publikováno v:
Journal of Biological Chemistry. 276:27498-27510
In the ferredoxin-NADP(+) reductase (FNR)/ferredoxin (Fd) system, an aromatic amino acid residue on the surface of Anabaena Fd, Phe-65, has been shown to be essential for the electron transfer (ET) reaction. We have investigated further the role of h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f85420c1ef4450e4ef748f713af85de
https://doi.org/10.1074/jbc.m102112200
https://doi.org/10.1074/jbc.m102112200
Autor:
Aida Herrerias, Laura Cecilia López, Nuria Marzo, Berta Pons, Marta José, Juan I. Jorquera, Merche Faro, Maite López
Publikováno v:
Biologicals : journal of the International Association of Biological Standardization. 41(6)
Studies have demonstrated that traces of activated factor XI (FXIa) present in specific brands of intravenous immunoglobulin (IVIG) concentrates may pose a thrombogenic risk.To characterize procoagulant activity during fractionation and the eliminati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae7ee75ec380234fb4a6c4f1306069e3
https://pubmed.ncbi.nlm.nih.gov/24051302
https://pubmed.ncbi.nlm.nih.gov/24051302
Publikováno v:
Bioelectrochemistry. 56:19-21
The enzyme Ferredoxin-NADP + reductase participates in the reductive side of the photosynthetic chain transferring electrons from reduced Ferredoxin (Fd) (or Flavodoxin (Fld)) to NADP + , a process that yields NADPH that can be used in many biosynthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b333efb96d39e703e78afcbf4d002296
https://doi.org/10.1016/s1567-5394(02)00039-7
https://doi.org/10.1016/s1567-5394(02)00039-7
Autor:
Merche, Faro, Burkhard, Schiffler, Achim, Heinz, Isabel, Nogués, Milagros, Medina, Rita, Bernhardt, Carlos, Gómez-Moreno
Publikováno v:
European journal of biochemistry. 270(4)
The opportunity to design enzymatic systems is becoming more feasible due to detailed knowledge of the structure of many proteins. As a first step, investigations have aimed to redesign already existing systems, so that they can perform a function di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8e46a217dcfcfcf3855cabc00b85ef84
https://pubmed.ncbi.nlm.nih.gov/12581212
https://pubmed.ncbi.nlm.nih.gov/12581212
Autor:
Merche, Faro, Susana, Frago, Tomas, Mayoral, Juan A, Hermoso, Julia, Sanz-Aparicio, Carlos, Gómez-Moreno, Milagros, Medina
Publikováno v:
European journal of biochemistry. 269(20)
The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e691e6258a9864fc2901d088285b7b48
https://pubmed.ncbi.nlm.nih.gov/12383252
https://pubmed.ncbi.nlm.nih.gov/12383252
Publikováno v:
European journal of biochemistry. 269(11)
Reduction potential determinations of K75E, E139K and E301A ferredoxin-NADP+ reductases provide valuable information concerning the factors that contribute to tune the flavin reduction potential. Thus, while E139 is not involved in such modulation, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::29c267df23e4d9855792b5abd88e4302
https://pubmed.ncbi.nlm.nih.gov/12047373
https://pubmed.ncbi.nlm.nih.gov/12047373