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%2F61388971%3A_____%2F14%3A00506700" target="_blank" >RIV/61388971:_____/14:00506700 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/14:10282872 RIV/00216208:11110/14:10282872

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0162013414001718?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0162013414001718?via%3Dihub</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 conducted in 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 found that (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 inhibited by superoxide dismutase and catalase. In a concordance with the result, the reactive oxygen species increased the CO generation, (iv) the E. coli cells overexpressing the L65N protein of YddV-heme also formed significant amounts of CO compared to the cells overexpressing the wild type protein (v) generation of verdoheme and CO was also observed for other mutants at Leu65 as well, but to a lesser extent Since Leu65 mutations are assumed to introduce the water molecule into the heme distal side of YddV-heme, it is suggested that the water molecule would significantly contribute to facilitating heme oxygenase reactions for the Leu65 mutants.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

<a href="/en/project/LO1509" target="_blank" >LO1509: Prague infrastructure for structural biology and metabolomics II</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2014

Confidentiality

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

Name of the periodical

Journal of Inorganic Biochemistry

ISSN

0162-0134

e-ISSN

—

Volume of the periodical

140

Issue of the periodical within the volume

NOV 2014

Country of publishing house

US - UNITED STATES

Number of pages

10

Pages from-to

29-38

UT code for WoS article

000342608900005

EID of the result in the Scopus database

2-s2.0-84904891340