About: Use of high pressure to study elementary steps in P450 and nitric oxide synthase

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Chemical reactions are often highly pressure-dependent. A perturbation of the elementary steps by pressure therefore offers the possibility of a detailed characterization of enzyme mechanisms. We used this method to study distinct steps in the reaction of nitric-oxide synthase (NOS), and compared them to analogous steps in the reaction of cytochrome P450 BM3 (BM3). Our results indicate that, in BM3, electron transfer depends on electrostatic interactions. In NOS, pressure, similarly to chemical denaturants, can mimick the structural effects of Ca/calmodulin. This helps to better understand the structural basis of the regulatory effect of Ca/calmodulin. Furthermore, stopped-flow kinetics under high pressure show that CO binding to the heme iron is hindered by substrate in NOS, but not in BM3. This indicates a relatively large or flexible substrate binding site in BM3, and a more narrow and rigid binding site in NOS. Chemical reactions are often highly pressure-dependent. A perturbation of the elementary steps by pressure therefore offers the possibility of a detailed characterization of enzyme mechanisms. We used this method to study distinct steps in the reaction of nitric-oxide synthase (NOS), and compared them to analogous steps in the reaction of cytochrome P450 BM3 (BM3). Our results indicate that, in BM3, electron transfer depends on electrostatic interactions. In NOS, pressure, similarly to chemical denaturants, can mimick the structural effects of Ca/calmodulin. This helps to better understand the structural basis of the regulatory effect of Ca/calmodulin. Furthermore, stopped-flow kinetics under high pressure show that CO binding to the heme iron is hindered by substrate in NOS, but not in BM3. This indicates a relatively large or flexible substrate binding site in BM3, and a more narrow and rigid binding site in NOS. (en) Chemické reakce jsou často závislé na vysokém tlaku.Tlak způsobuje odchylku základních kroků, proto se nabízí možnost detailně charakterizovat enzymové mechanismy. (cs)
Title	Use of high pressure to study elementary steps in P450 and nitric oxide synthase Use of high pressure to study elementary steps in P450 and nitric oxide synthase (en) Použití vysokého tlaku při studiu základních kroků syntázy P450 a oxidu dusného (cs)
skos:prefLabel	Use of high pressure to study elementary steps in P450 and nitric oxide synthase Use of high pressure to study elementary steps in P450 and nitric oxide synthase (en) Použití vysokého tlaku při studiu základních kroků syntázy P450 a oxidu dusného (cs)
skos:notation	RIV/61989592:15110/01:00006955!RIV09-MSM-15110___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA203/99/0277), Z(MSM 151100003)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2009
http://linked.open...aciTvurceVysledku	ANZENBACHER, Pavel
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Lékařská fakulta
http://linked.open...dnocenehoVysledku	699765
http://linked.open...ai/riv/idVysledku	RIV/61989592:15110/01:00006955
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Nitric-oxide synthase; Cytochrome P450; Calmodulin; High pressure; Electron transfer; CO binding (en)
http://linked.open.../riv/klicoveSlovo	Cytochrome P450 Electron transfer CO binding Nitric-oxide synthase High pressure Calmodulin
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[678A54180722]
http://linked.open...i/riv/nazevZdroje	Journal of Inorganic Biochemistry
http://linked.open...in/vavai/riv/obor	FR
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	Cytochrome P450 3A - key enzyme of drug metabolism. Comparison of the human enzyme and of the model system
http://linked.open...UplatneniVysledku	2001
http://linked.open...v/svazekPeriodika	87
http://linked.open...iv/tvurceVysledku	Anzenbacher, Pavel Lange, Reinhard Mayer, Bernd Bec, Nicole Gorren, Antonius C. F. Munro, A. W.
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20151100003
issn	0162-0134
number of pages	5 (xsd:int)
http://localhost/t...ganizacniJednotka	15110

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