Results 101 to 110 of about 135,211 (213)

Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase

, 2002
The gene fprA of Mycobacterium tuberculosis, encoding a putative protein with 40% identity to mammalian adrenodoxin reductase, was expressed in Escherichia coli and the protein purified to homogeneity.
F. Fischer, D. Raimondi, Debora Raimondi, G. Zanetti, A. Aliverti, Federico Fischer, Alessandro Aliverti, Giuliana Zanetti   +7 more
core   +1 more source

TAT-mediated transduction of bacterial redox proteins generates a cytoprotective effect on neuronal cells.

PLoS ONE, 2017
Cell penetrating peptides, also known as protein transduction domains, have the capacity to ubiquitously cross cellular membranes carrying many different cargos with negligible cytotoxicity.
Cecilia L Balaban, Claudia Banchio, Eduardo A Ceccarelli   +2 more
doaj   +1 more source

ferredoxin-like peptide original MUSCLE alignment.txt

, 2013
ferredoxin-like peptide original MUSCLE alignment ...
Leadbetter, Jared R., Lucey, Kaitlyn S., Kaitlyn S. Lucey (3315138), Jared R. Leadbetter (223388)   +3 more
core   +1 more source

Complex formation between ferredoxin and Synechococcus ferredoxin:nitrate oxidoreductase [PDF]

, 2004
The ferredoxin-dependent nitrate reductase from the cyanobacterium Synechococcus sp. PCC 7942 has been shown to form a high-affinity complex with ferredoxin at low ionic strength.
Li, Jun, Griffin, Jeannie L., Flores, Enrique, Hurley, John K., Tollin, Gordon, Herrero, Antonia, Knaff, David B., Hirasawa, Masakazu, Kim, Sung-Kun, Rubio, Luis M.   +9 more
core   +1 more source

New Light on Chloroplast Redox Regulation: Molecular Mechanism of Protein Thiol Oxidation

Frontiers in Plant Science, 2019
Thiol-based redox regulation is a posttranslational protein modification that plays a key role in adjusting chloroplast functions in response to changing light conditions.
Keisuke Yoshida, Yuichi Yokochi, Toru Hisabori   +2 more
doaj   +1 more source

Chemical cross-linking of ferredoxin to spinach thylakoids Evidence for two independent binding sites of ferredoxin to the membrane [PDF]

, 1987
Ferredoxin has been chemically cross-linked to thylakoids by using N-ethyl-3-(3-dimethylaminopropyl)-carbodiimide. The membranes thus treated became able to photoreduce cytochrome c and to catalyze the NADPH-cytochrome c reductase reaction without adding
Giuliana Merati, Zanetti, Giuliana, Merati, Giuliana, Giuliana Zanetti   +3 more
core   +1 more source

Two variants of the ferredoxin reductase (FDXR) causing isolated retinitis pigmentosa

Trends in Pediatrics
Objective: The FDXR gene encodesferredoxin reductase, which is a mitochondrial membrane protein and plays a role in Fe-S cluster synthesis. Loss of function in this gene causes intracellular iron accumulation, leading to dysfunction, especially in ...
Fayize Maden Bedel, Müşerref Başdemirci   +1 more
doaj   +1 more source

Ferredoxin-NADP+ reductase and ferredoxin of the protozoan parasite Toxoplasma gondii interact productively in vitro and in vivo

, 2002
Toxoplasma gondii possesses an apicoplast-localized, plant-type ferredoxin-NADP(+) reductase. We have cloned a [2Fe-2S] ferredoxin from the same parasite to investigate the interplay of the two redox proteins.
F. Seeber, V. Pandini, G. Zanetti, A. Aliverti, CAPRINI, GIANLUCA, N. Thomsen   +5 more
core   +1 more source

Biochemical characterization of ferredoxin-NADP+ reductase interaction with flavodoxin in Pseudomonas putida [PDF]

BMB Reports, 2012
Flavodoxin (Fld) has been demonstrated to bind to ferredoxin-NADP+ reductase A (FprA) in Pseudomonas putida. Tworesidues (Phe256, Lys259) of FprA are likely to be important forinteracting with Fld based on homology modeling.
nki Yeom & Woojun Park*
doaj  

Biochemical and crystallographyc characterization of ferredoxin-NADP+ reductase from nonphotosynthetic tissues

, 2001
Distinct forms of ferredoxin - NADP+ reductase are expressed in photosynthetic and nonphotosynthetic plant tissues. Both enzymes catalyze electron transfer between NADP(H) and ferredoxin; whereas in leaves the enzyme transfers reducing equivalents from ...
R. Faber, A. Negri, V. Pandini, G. Zanetti, A. Aliverti, C. M. Finnerty, P. A. Karplus, C. Ferioli   +7 more
core   +1 more source