The Roles of Thiolate-Heme Proteins, Other Than the P450 Cytochromes, in the Regulation of Heme-Sensor Proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F08%3A10283091" target="_blank" >RIV/00216208:11310/08:10283091 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The Roles of Thiolate-Heme Proteins, Other Than the P450 Cytochromes, in the Regulation of Heme-Sensor Proteins

Popis výsledku v původním jazyce

Cytochrome P450, nitric oxide synthase, and chloroperoxidase are typical thiolate-heme enzymes, in which heme iron coordinated with the cysteine thiolate activates molecular oxygen or hydrogen peroxide. A new group of thiolate-heme proteins is becoming recognized. In these proteins, termed heme-responsive/sensing proteins, or simply heme-sensor proteins, the thiolate-heme iron has a sensor function. All known heme-sensor proteins use a cysteine residue to bind heme. The first question is why cysteine isemployed in this capacity. Ligation of heme with thiolate, the presence of redox-dependent ligand switches, fast heme dissociation rates from the heme-sensor proteins, and formation of 5-coordinated NO-Fe(II) heme complexes, appear to be common characteristics of heme-sensor proteins. The Cys-Pro (CP) motif may also be important for heme binding in some heme-sensor proteins. In this minireview, we summarize the inorganic and physicochemical characters of heme-sensor proteins, and includ

Název v anglickém jazyce

The Roles of Thiolate-Heme Proteins, Other Than the P450 Cytochromes, in the Regulation of Heme-Sensor Proteins

Popis výsledku anglicky

Cytochrome P450, nitric oxide synthase, and chloroperoxidase are typical thiolate-heme enzymes, in which heme iron coordinated with the cysteine thiolate activates molecular oxygen or hydrogen peroxide. A new group of thiolate-heme proteins is becoming recognized. In these proteins, termed heme-responsive/sensing proteins, or simply heme-sensor proteins, the thiolate-heme iron has a sensor function. All known heme-sensor proteins use a cysteine residue to bind heme. The first question is why cysteine isemployed in this capacity. Ligation of heme with thiolate, the presence of redox-dependent ligand switches, fast heme dissociation rates from the heme-sensor proteins, and formation of 5-coordinated NO-Fe(II) heme complexes, appear to be common characteristics of heme-sensor proteins. The Cys-Pro (CP) motif may also be important for heme binding in some heme-sensor proteins. In this minireview, we summarize the inorganic and physicochemical characters of heme-sensor proteins, and includ

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2008

Kód důvěrnosti údajů

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

Název periodika

Acta Chimica Slovenica

ISSN

1318-0207

e-ISSN

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Svazek periodika

55

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

SI - Slovinská republika

Počet stran výsledku

8

Strana od-do

67-74

Kód UT WoS článku

000254379100009

EID výsledku v databázi Scopus

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