Gaseous O-2, NO, and CO in Signal Transduction: Structure and Function Relationships of Heme-Based Gas Sensors and Heme-Redox Sensors

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10315436" target="_blank" >RIV/00216208:11310/15:10315436 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/acs.chemrev.5b00018" target="_blank" >http://dx.doi.org/10.1021/acs.chemrev.5b00018</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.chemrev.5b00018" target="_blank" >10.1021/acs.chemrev.5b00018</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Gaseous O-2, NO, and CO in Signal Transduction: Structure and Function Relationships of Heme-Based Gas Sensors and Heme-Redox Sensors

Popis výsledku v původním jazyce

The heme iron complex is one of the most important cofactors in biological systems (Figure 1). The major functions of the heme iron complex are to serve as the O2 binding site for hemoglobin (O2 carrier protein), myoglobin (O2 storage protein), and cytochrome P450 (O2 activating enzyme); the peroxide activation site for peroxidase; and the electron transfer site for cytochromes.1MINUS SIGN 8 The heme iron complex in well-known heme proteins acts as the functional active center by virtue of its binding to an O2 molecule forming a heme ironMINUS SIGN O2 complex, which carries the O2 molecule to peripheral tissues as hemoglobin, stores the O2 molecule in muscle as myoglobin, and helps activate the O2 molecule by cleaving the OMINUS SIGN O bond in cytochrome P450 monooxygenase. Importantly, the O2 molecule binds only to heme Fe(II) complexes and not to heme Fe(III) complexes. For cytochromes, electrons are transferred to/from the partner protein via the heme iron complex, whereas for perox

Název v anglickém jazyce

Gaseous O-2, NO, and CO in Signal Transduction: Structure and Function Relationships of Heme-Based Gas Sensors and Heme-Redox Sensors

Popis výsledku anglicky

The heme iron complex is one of the most important cofactors in biological systems (Figure 1). The major functions of the heme iron complex are to serve as the O2 binding site for hemoglobin (O2 carrier protein), myoglobin (O2 storage protein), and cytochrome P450 (O2 activating enzyme); the peroxide activation site for peroxidase; and the electron transfer site for cytochromes.1MINUS SIGN 8 The heme iron complex in well-known heme proteins acts as the functional active center by virtue of its binding to an O2 molecule forming a heme ironMINUS SIGN O2 complex, which carries the O2 molecule to peripheral tissues as hemoglobin, stores the O2 molecule in muscle as myoglobin, and helps activate the O2 molecule by cleaving the OMINUS SIGN O bond in cytochrome P450 monooxygenase. Importantly, the O2 molecule binds only to heme Fe(II) complexes and not to heme Fe(III) complexes. For cytochromes, electrons are transferred to/from the partner protein via the heme iron complex, whereas for perox

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA15-19883S" target="_blank" >GA15-19883S: Mechanismus intraproteinového/mezidoménového přenosu signálu u modelových hemových senzorových proteinů</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Chemical Reviews

ISSN

0009-2665

e-ISSN

—

Svazek periodika

115

Číslo periodika v rámci svazku

13

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

43

Strana od-do

6491-6533

Kód UT WoS článku

000357963900005

EID výsledku v databázi Scopus

2-s2.0-84936077348