Catalytic enhancement of the heme-based oxygen-sensing phosphodiesterase EcDOS by hydrogen sulfide is caused by changes in heme coordination structure

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10314048" target="_blank" >RIV/00216208:11310/15:10314048 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00455109

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s10534-015-9847-7" target="_blank" >http://dx.doi.org/10.1007/s10534-015-9847-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10534-015-9847-7" target="_blank" >10.1007/s10534-015-9847-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Catalytic enhancement of the heme-based oxygen-sensing phosphodiesterase EcDOS by hydrogen sulfide is caused by changes in heme coordination structure

Popis výsledku v původním jazyce

EcDOS is a heme-based O-2-sensing phosphodiesterase in which O-2 binding to the heme iron complex in the N-terminal domain substantially enhances catalysis toward cyclic-di-GMP, which occurs in the C-terminal domain. Here, we found that hydrogen sulfideenhances the catalytic activity of full-length EcDOS, possibly owing to the admixture of 6-coordinated heme Fe(III)-SH- and Fe(II)-O-2 complexes generated during the reaction. Alanine substitution at Met95, the axial ligand for the heme Fe(II) complex, converted the heme Fe(III) complex into the heme Fe(III)-SH- complex, but the addition of Na2S did not further reduce it to the heme Fe(II) complex of the Met95Ala mutant, and no subsequent formation of the heme Fe(II)-O-2 complex was observed. In contrast, a Met95His mutant formed a stable heme Fe(II)-O-2 complex in response to the same treatment. An Arg97Glu mutant, containing a glutamate substitution at the amino acid that interacts with O-2 in the heme Fe(II)-O-2 complex, formed a sta

Název v anglickém jazyce

Catalytic enhancement of the heme-based oxygen-sensing phosphodiesterase EcDOS by hydrogen sulfide is caused by changes in heme coordination structure

Popis výsledku anglicky

EcDOS is a heme-based O-2-sensing phosphodiesterase in which O-2 binding to the heme iron complex in the N-terminal domain substantially enhances catalysis toward cyclic-di-GMP, which occurs in the C-terminal domain. Here, we found that hydrogen sulfideenhances the catalytic activity of full-length EcDOS, possibly owing to the admixture of 6-coordinated heme Fe(III)-SH- and Fe(II)-O-2 complexes generated during the reaction. Alanine substitution at Met95, the axial ligand for the heme Fe(II) complex, converted the heme Fe(III) complex into the heme Fe(III)-SH- complex, but the addition of Na2S did not further reduce it to the heme Fe(II) complex of the Met95Ala mutant, and no subsequent formation of the heme Fe(II)-O-2 complex was observed. In contrast, a Met95His mutant formed a stable heme Fe(II)-O-2 complex in response to the same treatment. An Arg97Glu mutant, containing a glutamate substitution at the amino acid that interacts with O-2 in the heme Fe(II)-O-2 complex, formed a sta

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

Biometals

ISSN

0966-0844

e-ISSN

—

Svazek periodika

28

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

16

Strana od-do

637-652

Kód UT WoS článku

000356877600004

EID výsledku v databázi Scopus

2-s2.0-84933277406