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Statements

Subject Item
n2:RIV%2F00216208%3A11110%2F09%3A4029%21RIV10-MSM-11110___
rdf:type
skos:Concept n17:Vysledek
dcterms:description
Nitric oxide synthases (NOSs) are unique flavohemoproteins with various roles in mammalian physiology. Constitutive NOS catalysis is initiated by fast hydride transfer from NADPH, followed by slower structural rearrangements. We used a photoactive nanotrigger (NT) to study the initial electron transfer to FAD in native neuronal NOS (nNOS) catalysis. Molecular modeling and fluorescence spectroscopy showed that selective NT binding to NADPH sites close to FAD is able to override Phe1395 regulation. Ultrafast injection of electrons into the protein electron pathway by NT photoactivation through the use of a femtosecond laser pulse is thus possible. We show that calmodulin, required for NO synthesis by constitutive NOS, strongly promotes intramolecular electron flow (6.2-fold stimulation) by a mechanism involving proton transfer to the reduced FAD(-) site. Site-directed mutagenesis using the S1176A and S1776T mutants of nNOS supports this hypothesis. Nitric oxide synthases (NOSs) are unique flavohemoproteins with various roles in mammalian physiology. Constitutive NOS catalysis is initiated by fast hydride transfer from NADPH, followed by slower structural rearrangements. We used a photoactive nanotrigger (NT) to study the initial electron transfer to FAD in native neuronal NOS (nNOS) catalysis. Molecular modeling and fluorescence spectroscopy showed that selective NT binding to NADPH sites close to FAD is able to override Phe1395 regulation. Ultrafast injection of electrons into the protein electron pathway by NT photoactivation through the use of a femtosecond laser pulse is thus possible. We show that calmodulin, required for NO synthesis by constitutive NOS, strongly promotes intramolecular electron flow (6.2-fold stimulation) by a mechanism involving proton transfer to the reduced FAD(-) site. Site-directed mutagenesis using the S1176A and S1776T mutants of nNOS supports this hypothesis.
dcterms:title
NO Formation by Neuronal NO-Synthase can be Controlled by Ultrafast Electron Injection from a Nanotrigger NO Formation by Neuronal NO-Synthase can be Controlled by Ultrafast Electron Injection from a Nanotrigger
skos:prefLabel
NO Formation by Neuronal NO-Synthase can be Controlled by Ultrafast Electron Injection from a Nanotrigger NO Formation by Neuronal NO-Synthase can be Controlled by Ultrafast Electron Injection from a Nanotrigger
skos:notation
RIV/00216208:11110/09:4029!RIV10-MSM-11110___
n3:aktivita
n14:Z n14:P
n3:aktivity
P(KAN200200651), Z(MSM0021620806)
n3:cisloPeriodika
4
n3:dodaniDat
n8:2010
n3:domaciTvurceVysledku
n12:4688678
n3:druhVysledku
n18:J
n3:duvernostUdaju
n13:S
n3:entitaPredkladatele
n9:predkladatel
n3:idSjednocenehoVysledku
329623
n3:idVysledku
RIV/00216208:11110/09:4029
n3:jazykVysledku
n19:eng
n3:klicovaSlova
emission spectroscopy; flavins; kinetics; metalloenzymes; molecular modeling; photocatalysis; nitric-oxide synthase; redox properties; structural basis; 2 flavins; domain; nadph; calmodulin; catalysis; reductase; binding
n3:klicoveSlovo
n4:2%20flavins n4:emission%20spectroscopy n4:binding n4:calmodulin n4:molecular%20modeling n4:nitric-oxide%20synthase n4:photocatalysis n4:metalloenzymes n4:reductase n4:flavins n4:structural%20basis n4:domain n4:kinetics n4:nadph n4:catalysis n4:redox%20properties
n3:kodStatuVydavatele
DE - Spolková republika Německo
n3:kontrolniKodProRIV
[E7FA14346C34]
n3:nazevZdroje
ChemBioChem
n3:obor
n7:CE
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
9
n3:projekt
n15:KAN200200651
n3:rokUplatneniVysledku
n8:2009
n3:svazekPeriodika
10
n3:tvurceVysledku
Martásek, Pavel Slama-Schwok, A. Blanchard-Desce, M. Lambry, JC Brochon, JC Deprez, E. Panda, SP van Faassen, EEH Beaumont, E.
n3:wos
000264168000014
n3:zamer
n10:MSM0021620806
s:issn
1439-4227
s:numberOfPages
12
n16:organizacniJednotka
11110