Introduction of water into the heme distal side by Leu65 mutations of an oxygen sensor, YddV, generates verdoheme and carbon monoxide, exerting the heme oxygenase reaction

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10282872" target="_blank" >RIV/00216208:11310/14:10282872 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11110/14:10282872 RIV/61388971:_____/14:00506700
Result on the web
<a href="http://dx.doi.org/10.1016/j.jinorgbio.2014.06.010" target="_blank" >http://dx.doi.org/10.1016/j.jinorgbio.2014.06.010</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jinorgbio.2014.06.010" target="_blank" >10.1016/j.jinorgbio.2014.06.010</a>

Result language
angličtina
Original language name
Introduction of water into the heme distal side by Leu65 mutations of an oxygen sensor, YddV, generates verdoheme and carbon monoxide, exerting the heme oxygenase reaction
Original language description
The globin-coupled oxygen sensor, YddV, is a heme-based oxygen sensor diguanylate cyclase. Oxygen binding to the heme Fe(II) complex in the N-terminal sensor domain of this enzyme substantially enhances its diguanylate cyclase activity which is conductedin the C-terminal functional domain. Leu65 is located on the heme distal side and is important for keeping the stability of the heme Fe(II)-O-2 complex by preventing the entry of the water molecule to the heme complex. In the present study, it was foundthat (i) Escherichia coli-overexpressed and purified L65N mutant of the isolated heme-bound domain of YddV (YddV-heme) contained the verdoheme iron complex and other modified heme complexes as determined by optical absorption spectroscopy and mass spectrometry; (ii) CO was generated in the reconstituted system composed of heme-bound L65N and NADPH:cytochrome P450 reductase as confirmed by gas chromatography; (iii) CO generation of heme-bound L65N in the reconstituted system was inhibite
Czech name
—
Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
<a href="/en/project/LO1509" target="_blank" >LO1509: Prague infrastructure for structural biology and metabolomics II</a><br>
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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