Spectroscopic characterization of the Co-substituted C-terminal domain of rubredoxin-2
rubredoxin-2 (Rxn2) is an essential member of the alkane hydroxylation pathway and transfers electrons from a reductase to the membrane-bound hydroxylase. The regioselective hydroxylation of linear alkanes is a challenging chemical transformation of great interest for the chemical industry. Herein,...
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| Veröffentlicht in: | Biological chemistry 2018-06, Vol.399 (7), p.787-798 |
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| container_title | Biological chemistry |
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| creator | Galle, Lisa M. Cutsail III, George E. Nischwitz, Volker DeBeer, Serena Span, Ingrid |
| description | rubredoxin-2 (Rxn2) is an essential member of the alkane hydroxylation pathway and transfers electrons from a reductase to the membrane-bound hydroxylase. The regioselective hydroxylation of linear alkanes is a challenging chemical transformation of great interest for the chemical industry. Herein, we report the preparation and spectroscopic characterization of cobalt-substituted
Rxn2 and a truncated version of the protein consisting of the C-terminal domain of the protein. Our spectroscopic data on the Co-substituted C-terminal domain supports a high-spin Co(II) with a distorted tetrahedral coordination environment. Investigation of the two-domain protein Rxn2 provides insights into the metal-binding properties of the N-terminal domain, the role of which is not well understood so far. Circular dichroism, electron paramagnetic resonance and X-ray absorption spectroscopies support an alternative Co-binding site within the N-terminal domain, which appears to not be relevant in nature. We have shown that chemical reconstitution in the presence of Co leads to incorporation of Co(II) into the active site of the C-terminal domain, but not the N-terminal domain of Rxn2 indicating distinct roles for the two rubredoxin domains. |
| doi_str_mv | 10.1515/hsz-2018-0142 |
| format | Article |
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Rxn2 and a truncated version of the protein consisting of the C-terminal domain of the protein. Our spectroscopic data on the Co-substituted C-terminal domain supports a high-spin Co(II) with a distorted tetrahedral coordination environment. Investigation of the two-domain protein Rxn2 provides insights into the metal-binding properties of the N-terminal domain, the role of which is not well understood so far. Circular dichroism, electron paramagnetic resonance and X-ray absorption spectroscopies support an alternative Co-binding site within the N-terminal domain, which appears to not be relevant in nature. We have shown that chemical reconstitution in the presence of Co leads to incorporation of Co(II) into the active site of the C-terminal domain, but not the N-terminal domain of Rxn2 indicating distinct roles for the two rubredoxin domains.</description><identifier>ISSN: 1431-6730</identifier><identifier>EISSN: 1437-4315</identifier><identifier>DOI: 10.1515/hsz-2018-0142</identifier><identifier>PMID: 29894292</identifier><language>eng</language><publisher>Germany: De Gruyter</publisher><subject>Alkanes ; AlkG ; Binding sites ; Catalytic Domain ; Chemical industry ; Circular Dichroism ; Cobalt ; Cobalt - chemistry ; Cobalt - metabolism ; Dichroism ; Electron paramagnetic resonance ; Electron spin resonance ; Electron Spin Resonance Spectroscopy ; GPo1 ; Hydroxylase ; Hydroxylation ; iron-sulfur protein ; metal substitution ; Organic chemistry ; Proteins ; Pseudomonas putida ; Pseudomonas putida - chemistry ; Reductase ; Reductases ; rubredoxin ; Rubredoxins - chemistry ; Rubredoxins - metabolism ; Spectrometry, X-Ray Emission ; Spectrophotometry, Ultraviolet ; Spectroscopy ; Substitutes ; X ray absorption</subject><ispartof>Biological chemistry, 2018-06, Vol.399 (7), p.787-798</ispartof><rights>Copyright Walter de Gruyter GmbH 2018</rights><rights>2018 Walter de Gruyter GmbH, Berlin/Boston</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-a85f14d7df352638badbce6bbd34230f1db0eb481a2cf4a2936a5a37b6393cad3</citedby><cites>FETCH-LOGICAL-c441t-a85f14d7df352638badbce6bbd34230f1db0eb481a2cf4a2936a5a37b6393cad3</cites><orcidid>0000-0002-2892-4825</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.degruyter.com/document/doi/10.1515/hsz-2018-0142/pdf$$EPDF$$P50$$Gwalterdegruyter$$H</linktopdf><linktohtml>$$Uhttps://www.degruyter.com/document/doi/10.1515/hsz-2018-0142/html$$EHTML$$P50$$Gwalterdegruyter$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,66497,68281</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29894292$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Galle, Lisa M.</creatorcontrib><creatorcontrib>Cutsail III, George E.</creatorcontrib><creatorcontrib>Nischwitz, Volker</creatorcontrib><creatorcontrib>DeBeer, Serena</creatorcontrib><creatorcontrib>Span, Ingrid</creatorcontrib><title>Spectroscopic characterization of the Co-substituted C-terminal domain of rubredoxin-2</title><title>Biological chemistry</title><addtitle>Biol Chem</addtitle><description>rubredoxin-2 (Rxn2) is an essential member of the alkane hydroxylation pathway and transfers electrons from a reductase to the membrane-bound hydroxylase. The regioselective hydroxylation of linear alkanes is a challenging chemical transformation of great interest for the chemical industry. Herein, we report the preparation and spectroscopic characterization of cobalt-substituted
Rxn2 and a truncated version of the protein consisting of the C-terminal domain of the protein. Our spectroscopic data on the Co-substituted C-terminal domain supports a high-spin Co(II) with a distorted tetrahedral coordination environment. Investigation of the two-domain protein Rxn2 provides insights into the metal-binding properties of the N-terminal domain, the role of which is not well understood so far. Circular dichroism, electron paramagnetic resonance and X-ray absorption spectroscopies support an alternative Co-binding site within the N-terminal domain, which appears to not be relevant in nature. We have shown that chemical reconstitution in the presence of Co leads to incorporation of Co(II) into the active site of the C-terminal domain, but not the N-terminal domain of Rxn2 indicating distinct roles for the two rubredoxin domains.</description><subject>Alkanes</subject><subject>AlkG</subject><subject>Binding sites</subject><subject>Catalytic Domain</subject><subject>Chemical industry</subject><subject>Circular Dichroism</subject><subject>Cobalt</subject><subject>Cobalt - chemistry</subject><subject>Cobalt - metabolism</subject><subject>Dichroism</subject><subject>Electron paramagnetic resonance</subject><subject>Electron spin resonance</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>GPo1</subject><subject>Hydroxylase</subject><subject>Hydroxylation</subject><subject>iron-sulfur protein</subject><subject>metal substitution</subject><subject>Organic chemistry</subject><subject>Proteins</subject><subject>Pseudomonas putida</subject><subject>Pseudomonas putida - chemistry</subject><subject>Reductase</subject><subject>Reductases</subject><subject>rubredoxin</subject><subject>Rubredoxins - chemistry</subject><subject>Rubredoxins - metabolism</subject><subject>Spectrometry, X-Ray Emission</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spectroscopy</subject><subject>Substitutes</subject><subject>X ray absorption</subject><issn>1431-6730</issn><issn>1437-4315</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90ctrFTEUBvAgin3o0q0MuHGTmuQkkwS6kYu2hYILH9shr-lNmbm5Jhls-9eb29sqFHGVs_jxHXI-hN5QckIFFR_W5Q4zQhUmlLNn6JBykJgDFc_vZ4p7CeQAHZVyTQhRhMNLdMC00pxpdoh-fN0GV3MqLm2j69zaZONqyPHO1Jg2XRq7ug7dKuGy2FJjXWrw3Qo3MseNmTqfZhPvXV5sDj7dxA1mr9CL0UwlvH54j9H3z5--rc7x5Zezi9XHS-w4pxUbJUbKvfQjCNaDssZbF3prPXAGZKTekmC5ooa5kRumoTfCgLQ9aHDGwzF6v8_d5vRzCaUOcywuTJPZhLSUgRHBNbBekUbfPaHXacntC001Q2mvuPivIhIEaClkU3ivXLtcyWEctjnOJt8OlAy7WoZWy7CrZdjV0vzbh9TFzsH_0Y89NHC6B7_M1E7rw1Vebtvwd_u_g7WWUkn4DT20m9Y</recordid><startdate>20180627</startdate><enddate>20180627</enddate><creator>Galle, Lisa M.</creator><creator>Cutsail III, George E.</creator><creator>Nischwitz, Volker</creator><creator>DeBeer, Serena</creator><creator>Span, Ingrid</creator><general>De Gruyter</general><general>Walter de Gruyter GmbH</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>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-2892-4825</orcidid></search><sort><creationdate>20180627</creationdate><title>Spectroscopic characterization of the Co-substituted C-terminal domain of rubredoxin-2</title><author>Galle, Lisa M. ; Cutsail III, George E. ; Nischwitz, Volker ; DeBeer, Serena ; Span, Ingrid</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-a85f14d7df352638badbce6bbd34230f1db0eb481a2cf4a2936a5a37b6393cad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Alkanes</topic><topic>AlkG</topic><topic>Binding sites</topic><topic>Catalytic Domain</topic><topic>Chemical industry</topic><topic>Circular Dichroism</topic><topic>Cobalt</topic><topic>Cobalt - chemistry</topic><topic>Cobalt - metabolism</topic><topic>Dichroism</topic><topic>Electron paramagnetic resonance</topic><topic>Electron spin resonance</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>GPo1</topic><topic>Hydroxylase</topic><topic>Hydroxylation</topic><topic>iron-sulfur protein</topic><topic>metal substitution</topic><topic>Organic chemistry</topic><topic>Proteins</topic><topic>Pseudomonas putida</topic><topic>Pseudomonas putida - chemistry</topic><topic>Reductase</topic><topic>Reductases</topic><topic>rubredoxin</topic><topic>Rubredoxins - chemistry</topic><topic>Rubredoxins - metabolism</topic><topic>Spectrometry, X-Ray Emission</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Spectroscopy</topic><topic>Substitutes</topic><topic>X ray absorption</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Galle, Lisa M.</creatorcontrib><creatorcontrib>Cutsail III, George E.</creatorcontrib><creatorcontrib>Nischwitz, Volker</creatorcontrib><creatorcontrib>DeBeer, Serena</creatorcontrib><creatorcontrib>Span, Ingrid</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Galle, Lisa M.</au><au>Cutsail III, George E.</au><au>Nischwitz, Volker</au><au>DeBeer, Serena</au><au>Span, Ingrid</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spectroscopic characterization of the Co-substituted C-terminal domain of rubredoxin-2</atitle><jtitle>Biological chemistry</jtitle><addtitle>Biol Chem</addtitle><date>2018-06-27</date><risdate>2018</risdate><volume>399</volume><issue>7</issue><spage>787</spage><epage>798</epage><pages>787-798</pages><issn>1431-6730</issn><eissn>1437-4315</eissn><abstract>rubredoxin-2 (Rxn2) is an essential member of the alkane hydroxylation pathway and transfers electrons from a reductase to the membrane-bound hydroxylase. The regioselective hydroxylation of linear alkanes is a challenging chemical transformation of great interest for the chemical industry. Herein, we report the preparation and spectroscopic characterization of cobalt-substituted
Rxn2 and a truncated version of the protein consisting of the C-terminal domain of the protein. Our spectroscopic data on the Co-substituted C-terminal domain supports a high-spin Co(II) with a distorted tetrahedral coordination environment. Investigation of the two-domain protein Rxn2 provides insights into the metal-binding properties of the N-terminal domain, the role of which is not well understood so far. Circular dichroism, electron paramagnetic resonance and X-ray absorption spectroscopies support an alternative Co-binding site within the N-terminal domain, which appears to not be relevant in nature. We have shown that chemical reconstitution in the presence of Co leads to incorporation of Co(II) into the active site of the C-terminal domain, but not the N-terminal domain of Rxn2 indicating distinct roles for the two rubredoxin domains.</abstract><cop>Germany</cop><pub>De Gruyter</pub><pmid>29894292</pmid><doi>10.1515/hsz-2018-0142</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-2892-4825</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alkanes AlkG Binding sites Catalytic Domain Chemical industry Circular Dichroism Cobalt Cobalt - chemistry Cobalt - metabolism Dichroism Electron paramagnetic resonance Electron spin resonance Electron Spin Resonance Spectroscopy GPo1 Hydroxylase Hydroxylation iron-sulfur protein metal substitution Organic chemistry Proteins Pseudomonas putida Pseudomonas putida - chemistry Reductase Reductases rubredoxin Rubredoxins - chemistry Rubredoxins - metabolism Spectrometry, X-Ray Emission Spectrophotometry, Ultraviolet Spectroscopy Substitutes X ray absorption |
| title | Spectroscopic characterization of the Co-substituted C-terminal domain of rubredoxin-2 |
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