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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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. |
doi_str_mv | 10.1007/s10534-016-9947-z |
format | Article |
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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.</description><identifier>ISSN: 0966-0844</identifier><identifier>EISSN: 1572-8773</identifier><identifier>DOI: 10.1007/s10534-016-9947-z</identifier><identifier>PMID: 27395436</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>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</subject><ispartof>Biometals, 2016-08, Vol.29 (4), p.715-729</ispartof><rights>Springer Science+Business Media New York 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-1597e3018866cbd3a3a126d52edd4a84098c0bfa1773996cdbbf0f5549a1b21a3</citedby><cites>FETCH-LOGICAL-c438t-1597e3018866cbd3a3a126d52edd4a84098c0bfa1773996cdbbf0f5549a1b21a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10534-016-9947-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10534-016-9947-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27929,27930,41493,42562,51324</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27395436$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fojtikova, Veronika</creatorcontrib><creatorcontrib>Bartosova, Martina</creatorcontrib><creatorcontrib>Man, Petr</creatorcontrib><creatorcontrib>Stranava, Martin</creatorcontrib><creatorcontrib>Shimizu, Toru</creatorcontrib><creatorcontrib>Martinkova, Marketa</creatorcontrib><title>Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK</title><title>Biometals</title><addtitle>Biometals</addtitle><addtitle>Biometals</addtitle><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.</description><subject>Binding</subject><subject>Biocatalysis - drug effects</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Cell Biology</subject><subject>Enzymatic activity</subject><subject>Heme - chemistry</subject><subject>Heme - metabolism</subject><subject>Histidine</subject><subject>Histidine Kinase - chemistry</subject><subject>Histidine Kinase - genetics</subject><subject>Histidine Kinase - metabolism</subject><subject>Hydrogen sulfide</subject><subject>Hydrogen Sulfide - chemistry</subject><subject>Hydrogen Sulfide - pharmacology</subject><subject>Iron</subject><subject>Kinases</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>Medicine/Public Health</subject><subject>Microbiology</subject><subject>Molecular Structure</subject><subject>Mutagenesis, Site-Directed</subject><subject>Myxococcales - enzymology</subject><subject>Oxygen</subject><subject>Oxygen - chemistry</subject><subject>Oxygen - metabolism</subject><subject>Oxygen probes</subject><subject>Pharmacology/Toxicology</subject><subject>Phosphorylation - drug effects</subject><subject>Plant Physiology</subject><subject>Proteins</subject><subject>Residues</subject><subject>Signal transduction</subject><issn>0966-0844</issn><issn>1572-8773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkU1rFTEUhoMo9lr9AW4k4MZNNJl8TZal1FYsuNF1yOTj3pS5k2uSEacrf3ozvVVEELoKJO95cs55AHhN8HuCsfxQCOaUIUwEUopJdPsEbAiXHeqlpE_BBishEO4ZOwEvSrnBGCuJxXNw0kmqOKNiA35dhOBtLTAFuFtcTls_wTKPIToP0wTrzsOd33toU8ouTqbGdltqnm2ds4dmctCaasalRguNrfFHrMtKWyu3YxrihGyaD6N3MP1c7vF-KinDs3Bprz6_BM-CGYt_9XCegm8fL76eX6HrL5efzs-ukWW0r4hwJT3FpO-FsIOjhhrSCcc77xwzPcOqt3gIhrTJlRLWDUPAgXOmDBk6YugpeHfkHnL6PvtS9T4W68fRTD7NRZOeckGVZOoR0bbkdfX8EdHmoHXd0RZ9-0_0Js15ajOvwGamNbsCyTFlcyol-6APOe5NXjTBepWuj9J1k65X6fq21bx5IM_D3rs_Fb8tt0B3DJT2NG19_uvr_1LvAJ0euCA</recordid><startdate>20160801</startdate><enddate>20160801</enddate><creator>Fojtikova, Veronika</creator><creator>Bartosova, Martina</creator><creator>Man, Petr</creator><creator>Stranava, Martin</creator><creator>Shimizu, Toru</creator><creator>Martinkova, Marketa</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7U5</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20160801</creationdate><title>Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK</title><author>Fojtikova, Veronika ; Bartosova, Martina ; Man, Petr ; Stranava, Martin ; Shimizu, Toru ; Martinkova, Marketa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-1597e3018866cbd3a3a126d52edd4a84098c0bfa1773996cdbbf0f5549a1b21a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Binding</topic><topic>Biocatalysis - drug effects</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Catalysis</topic><topic>Catalytic activity</topic><topic>Cell Biology</topic><topic>Enzymatic activity</topic><topic>Heme - chemistry</topic><topic>Heme - metabolism</topic><topic>Histidine</topic><topic>Histidine Kinase - chemistry</topic><topic>Histidine Kinase - genetics</topic><topic>Histidine Kinase - metabolism</topic><topic>Hydrogen sulfide</topic><topic>Hydrogen Sulfide - chemistry</topic><topic>Hydrogen Sulfide - pharmacology</topic><topic>Iron</topic><topic>Kinases</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Ligands</topic><topic>Medicine/Public Health</topic><topic>Microbiology</topic><topic>Molecular Structure</topic><topic>Mutagenesis, Site-Directed</topic><topic>Myxococcales - enzymology</topic><topic>Oxygen</topic><topic>Oxygen - chemistry</topic><topic>Oxygen - metabolism</topic><topic>Oxygen probes</topic><topic>Pharmacology/Toxicology</topic><topic>Phosphorylation - drug effects</topic><topic>Plant Physiology</topic><topic>Proteins</topic><topic>Residues</topic><topic>Signal transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fojtikova, Veronika</creatorcontrib><creatorcontrib>Bartosova, Martina</creatorcontrib><creatorcontrib>Man, Petr</creatorcontrib><creatorcontrib>Stranava, Martin</creatorcontrib><creatorcontrib>Shimizu, Toru</creatorcontrib><creatorcontrib>Martinkova, Marketa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Biometals</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fojtikova, Veronika</au><au>Bartosova, Martina</au><au>Man, Petr</au><au>Stranava, Martin</au><au>Shimizu, Toru</au><au>Martinkova, Marketa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of hydrogen sulfide on the heme coordination structure and catalytic activity of the globin-coupled oxygen sensor AfGcHK</atitle><jtitle>Biometals</jtitle><stitle>Biometals</stitle><addtitle>Biometals</addtitle><date>2016-08-01</date><risdate>2016</risdate><volume>29</volume><issue>4</issue><spage>715</spage><epage>729</epage><pages>715-729</pages><issn>0966-0844</issn><eissn>1572-8773</eissn><abstract>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.</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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