Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS)

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F13%3A00422909" target="_blank" >RIV/61388971:_____/13:00422909 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/13:10191633

Result on the web

<a href="http://dx.doi.org/10.1007/s10534-013-9640-4" target="_blank" >http://dx.doi.org/10.1007/s10534-013-9640-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10534-013-9640-4" target="_blank" >10.1007/s10534-013-9640-4</a>

Result language

angličtina

Original language name

Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS)

Original language description

The heme-based oxygen-sensor phosphodiesterase from Escherichia coli (Ec DOS), is composed of an N-terminal heme-bound oxygen sensing domain and a C-terminal catalytic domain. Oxygen (O-2) binding to the heme Fe(II) complex in Ec DOS substantially enhances catalysis. Addition of hydrogen sulfide (H2S) to the heme Fe(III) complex in Ec DOS also remarkably stimulates catalysis in part due to the heme Fe(III)-SH and heme Fe(II)-O-2 complexes formed by H2S. In this study, we examined the roles of the heme distal amino acids, M95 (the axial ligand of the heme Fe(II) complex) and R97 (the O-2 binding site in the heme Fe(II)-O-2 complex) of the isolated heme-binding domain of Ec DOS (Ec DOS-PAS) in the binding of H2S under aerobic conditions. Interestingly, R97A and R97I mutant proteins formed an oxygen-incorporated modified heme, verdoheme, following addition of H2S combined with H2O2 generated by the reactions. Time-dependent mass spectroscopic data corroborated the findings. In contrast, H

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2013

Confidentiality

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

Name of the periodical

Biometals

ISSN

0966-0844

e-ISSN

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Volume of the periodical

26

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

839-852

UT code for WoS article

000326926600017

EID of the result in the Scopus database

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