Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK

Af GcHK is a globin-coupled histidine kinase that is one component of a two-component signal transduction system. The catalytic activity of this heme-based oxygen sensor is due to its C-terminal kinase domain and is strongly stimulated by the binding of O 2 or CO to the heme Fe(II) complex in the N-...

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Veröffentlicht in:Biometals 2016-08, Vol.29 (4), p.715-729
Hauptverfasser: Fojtikova, Veronika, Bartosova, Martina, Man, Petr, Stranava, Martin, Shimizu, Toru, Martinkova, Marketa
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container_issue 4
container_start_page 715
container_title Biometals
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creator Fojtikova, Veronika
Bartosova, Martina
Man, Petr
Stranava, Martin
Shimizu, Toru
Martinkova, Marketa
description Af GcHK is a globin-coupled histidine kinase that is one component of a two-component signal transduction system. The catalytic activity of this heme-based oxygen sensor is due to its C-terminal kinase domain and is strongly stimulated by the binding of O 2 or CO to the heme Fe(II) complex in the N-terminal oxygen sensing domain. Hydrogen sulfide (H 2 S) is an important gaseous signaling molecule and can serve as a heme axial ligand, but its interactions with heme-based oxygen sensors have not been studied as extensively as those of O 2 , CO, and NO. To address this knowledge gap, we investigated the effects of H 2 S binding on the heme coordination structure and catalytic activity of wild-type Af GcHK and mutants in which residues at the putative O 2 -binding site (Tyr45) or the heme distal side (Leu68) were substituted. Adding Na 2 S to the initial OH-bound 6-coordinate Fe(III) low-spin complexes transformed them into SH-bound 6-coordinate Fe(III) low-spin complexes. The Leu68 mutants also formed a small proportion of verdoheme under these conditions. Conversely, when the heme-based oxygen sensor Ec DOS was treated with Na 2 S, the initially formed Fe(III)–SH heme complex was quickly converted into Fe(II) and Fe(II)–O 2 complexes. Interestingly, the autophosphorylation activity of the heme Fe(III)–SH complex was not significantly different from the maximal enzyme activity of Af GcHK (containing the heme Fe(III)–OH complex), whereas in the case of Ec DOS the changes in coordination caused by Na 2 S treatment led to remarkable increases in catalytic activity.
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The catalytic activity of this heme-based oxygen sensor is due to its C-terminal kinase domain and is strongly stimulated by the binding of O 2 or CO to the heme Fe(II) complex in the N-terminal oxygen sensing domain. Hydrogen sulfide (H 2 S) is an important gaseous signaling molecule and can serve as a heme axial ligand, but its interactions with heme-based oxygen sensors have not been studied as extensively as those of O 2 , CO, and NO. To address this knowledge gap, we investigated the effects of H 2 S binding on the heme coordination structure and catalytic activity of wild-type Af GcHK and mutants in which residues at the putative O 2 -binding site (Tyr45) or the heme distal side (Leu68) were substituted. Adding Na 2 S to the initial OH-bound 6-coordinate Fe(III) low-spin complexes transformed them into SH-bound 6-coordinate Fe(III) low-spin complexes. The Leu68 mutants also formed a small proportion of verdoheme under these conditions. Conversely, when the heme-based oxygen sensor Ec DOS was treated with Na 2 S, the initially formed Fe(III)–SH heme complex was quickly converted into Fe(II) and Fe(II)–O 2 complexes. Interestingly, the autophosphorylation activity of the heme Fe(III)–SH complex was not significantly different from the maximal enzyme activity of Af GcHK (containing the heme Fe(III)–OH complex), whereas in the case of Ec DOS the changes in coordination caused by Na 2 S treatment led to remarkable increases in catalytic activity.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>27395436</pmid><doi>10.1007/s10534-016-9947-z</doi><tpages>15</tpages></addata></record>
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subjects Binding
Biocatalysis - drug effects
Biochemistry
Biomedical and Life Sciences
Catalysis
Catalytic activity
Cell Biology
Enzymatic activity
Heme - chemistry
Heme - metabolism
Histidine
Histidine Kinase - chemistry
Histidine Kinase - genetics
Histidine Kinase - metabolism
Hydrogen sulfide
Hydrogen Sulfide - chemistry
Hydrogen Sulfide - pharmacology
Iron
Kinases
Kinetics
Life Sciences
Ligands
Medicine/Public Health
Microbiology
Molecular Structure
Mutagenesis, Site-Directed
Myxococcales - enzymology
Oxygen
Oxygen - chemistry
Oxygen - metabolism
Oxygen probes
Pharmacology/Toxicology
Phosphorylation - drug effects
Plant Physiology
Proteins
Residues
Signal transduction
title Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK
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