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Substitution of Valine for Histidine 265 in Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum Affects Activity and Spectroscopic States
In carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum , histidine 265 was replaced with valine by site-directed mutagenesis of the cooS gene. The altered form of CODH (H265V) had a low nickel content and a dramatically reduced level of catalytic activity. Although treatment with NiCl 2...
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| Published in: | The Journal of biological chemistry 1998-02, Vol.273 (7), p.4059-4064 |
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| Main Authors: | , , , , , |
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| container_end_page | 4064 |
| container_issue | 7 |
| container_start_page | 4059 |
| container_title | The Journal of biological chemistry |
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| creator | Spangler, N J Meyers, M R Gierke, K L Kerby, R L Roberts, G P Ludden, P W |
| description | In carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum , histidine 265 was replaced with valine by site-directed mutagenesis of the cooS gene. The altered form of CODH (H265V) had a low nickel content and a dramatically reduced level of catalytic activity. Although
treatment with NiCl 2 and CoCl 2 increased the activity of H265V CODH by severalfold, activity levels remained more than 1000-fold lower than that of wild-type
CODH. Histidine 265 was not essential for the formation and stability of the Fe 4 S 4 clusters. The K
m and K
D for CO as well as the K
D for cyanide were relatively unchanged as a result of the amino acid substitution in CODH. The time-dependent reduction of
the [Fe 4 S 4 ] 2+ clusters by CO occurred on a time scale of hours, suggesting that, as a consequence of the mutation, a rate-limiting step
had been introduced prior to the transfer of electrons from CO to the cubanes in centers B and C. EPR spectra of H265V CODH
lacked the g av = 1.86 and g av = 1.87 signals characteristic of reduced forms of the active site (center C) of wild-type CODH. This indicates that the electronic
properties of center C have been modified possibly by the disruption or alteration of the ligand-mediated interaction between
the nickel site and Fe 4 S 4 chromophore. |
| doi_str_mv | 10.1074/jbc.273.7.4059 |
| format | article |
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treatment with NiCl 2 and CoCl 2 increased the activity of H265V CODH by severalfold, activity levels remained more than 1000-fold lower than that of wild-type
CODH. Histidine 265 was not essential for the formation and stability of the Fe 4 S 4 clusters. The K
m and K
D for CO as well as the K
D for cyanide were relatively unchanged as a result of the amino acid substitution in CODH. The time-dependent reduction of
the [Fe 4 S 4 ] 2+ clusters by CO occurred on a time scale of hours, suggesting that, as a consequence of the mutation, a rate-limiting step
had been introduced prior to the transfer of electrons from CO to the cubanes in centers B and C. EPR spectra of H265V CODH
lacked the g av = 1.86 and g av = 1.87 signals characteristic of reduced forms of the active site (center C) of wild-type CODH. This indicates that the electronic
properties of center C have been modified possibly by the disruption or alteration of the ligand-mediated interaction between
the nickel site and Fe 4 S 4 chromophore.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.273.7.4059</identifier><identifier>PMID: 9461598</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Aldehyde Oxidoreductases - chemistry ; Aldehyde Oxidoreductases - metabolism ; Binding Sites ; Carbon Monoxide - metabolism ; Cobalt - pharmacology ; Cyanides - metabolism ; Electron Spin Resonance Spectroscopy ; Iron - analysis ; Iron-Sulfur Proteins - genetics ; Iron-Sulfur Proteins - metabolism ; Multienzyme Complexes - chemistry ; Multienzyme Complexes - metabolism ; Mutagenesis, Site-Directed - genetics ; Nickel - analysis ; Nickel - pharmacology ; Rhodospirillum rubrum - enzymology</subject><ispartof>The Journal of biological chemistry, 1998-02, Vol.273 (7), p.4059-4064</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-cbdb7412120de74a1a13b3844d25a222c77a18c69c56381c9db482ee02727ddb3</citedby><cites>FETCH-LOGICAL-c454t-cbdb7412120de74a1a13b3844d25a222c77a18c69c56381c9db482ee02727ddb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9461598$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Spangler, N J</creatorcontrib><creatorcontrib>Meyers, M R</creatorcontrib><creatorcontrib>Gierke, K L</creatorcontrib><creatorcontrib>Kerby, R L</creatorcontrib><creatorcontrib>Roberts, G P</creatorcontrib><creatorcontrib>Ludden, P W</creatorcontrib><title>Substitution of Valine for Histidine 265 in Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum Affects Activity and Spectroscopic States</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>In carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum , histidine 265 was replaced with valine by site-directed mutagenesis of the cooS gene. The altered form of CODH (H265V) had a low nickel content and a dramatically reduced level of catalytic activity. Although
treatment with NiCl 2 and CoCl 2 increased the activity of H265V CODH by severalfold, activity levels remained more than 1000-fold lower than that of wild-type
CODH. Histidine 265 was not essential for the formation and stability of the Fe 4 S 4 clusters. The K
m and K
D for CO as well as the K
D for cyanide were relatively unchanged as a result of the amino acid substitution in CODH. The time-dependent reduction of
the [Fe 4 S 4 ] 2+ clusters by CO occurred on a time scale of hours, suggesting that, as a consequence of the mutation, a rate-limiting step
had been introduced prior to the transfer of electrons from CO to the cubanes in centers B and C. EPR spectra of H265V CODH
lacked the g av = 1.86 and g av = 1.87 signals characteristic of reduced forms of the active site (center C) of wild-type CODH. This indicates that the electronic
properties of center C have been modified possibly by the disruption or alteration of the ligand-mediated interaction between
the nickel site and Fe 4 S 4 chromophore.</description><subject>Aldehyde Oxidoreductases - chemistry</subject><subject>Aldehyde Oxidoreductases - metabolism</subject><subject>Binding Sites</subject><subject>Carbon Monoxide - metabolism</subject><subject>Cobalt - pharmacology</subject><subject>Cyanides - metabolism</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Iron - analysis</subject><subject>Iron-Sulfur Proteins - genetics</subject><subject>Iron-Sulfur Proteins - metabolism</subject><subject>Multienzyme Complexes - chemistry</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Mutagenesis, Site-Directed - genetics</subject><subject>Nickel - analysis</subject><subject>Nickel - pharmacology</subject><subject>Rhodospirillum rubrum - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNpNUU1v1DAQtRBVWQpXbkgWB24JtuPEyXG1fBSpqFIXEDfLH5PGVRIH2wH2T_Q349WuEHN5mnlvnkbzEHpFSUmJ4O8etCmZqEpRclJ3T9CGkrYqqpr-eIo2hDBadKxun6HnMT6QXLyjl-iy4w2tu3aDHverjsmlNTk_Y9_j72p0M-DeB3ztMmOPHWtq7Ga8U0Fn1Rc_-z_OAn4Pw8EGfw-zinkl-AnfDd76uLjgxnGdcFh1yLDtezAp4q1J7pdLB6xmi_dLngUfjV-cwfukEsQX6KJXY4SXZ7xC3z5--Lq7Lm5uP33ebW8Kw2ueCqOtFpwyyogFwRVVtNJVy7lltWKMGSEUbU3TmbqpWmo6q3nLAAgTTFirqyv09uS7BP9zhZjk5KKBcVQz-DVK2jDBG06ysDwJTb40BujlEtykwkFSIo8ByByAzAFIIY8B5IXXZ-dVT2D_yc8fz_ybEz-4--G3CyC182aA6X-Tv70Gjzw</recordid><startdate>19980213</startdate><enddate>19980213</enddate><creator>Spangler, N J</creator><creator>Meyers, M R</creator><creator>Gierke, K L</creator><creator>Kerby, R L</creator><creator>Roberts, G P</creator><creator>Ludden, P W</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>C1K</scope></search><sort><creationdate>19980213</creationdate><title>Substitution of Valine for Histidine 265 in Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum Affects Activity and Spectroscopic States</title><author>Spangler, N J ; Meyers, M R ; Gierke, K L ; Kerby, R L ; Roberts, G P ; Ludden, P W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-cbdb7412120de74a1a13b3844d25a222c77a18c69c56381c9db482ee02727ddb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Aldehyde Oxidoreductases - chemistry</topic><topic>Aldehyde Oxidoreductases - metabolism</topic><topic>Binding Sites</topic><topic>Carbon Monoxide - metabolism</topic><topic>Cobalt - pharmacology</topic><topic>Cyanides - metabolism</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Iron - analysis</topic><topic>Iron-Sulfur Proteins - genetics</topic><topic>Iron-Sulfur Proteins - metabolism</topic><topic>Multienzyme Complexes - chemistry</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Mutagenesis, Site-Directed - genetics</topic><topic>Nickel - analysis</topic><topic>Nickel - pharmacology</topic><topic>Rhodospirillum rubrum - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spangler, N J</creatorcontrib><creatorcontrib>Meyers, M R</creatorcontrib><creatorcontrib>Gierke, K L</creatorcontrib><creatorcontrib>Kerby, R L</creatorcontrib><creatorcontrib>Roberts, G P</creatorcontrib><creatorcontrib>Ludden, P W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Spangler, N J</au><au>Meyers, M R</au><au>Gierke, K L</au><au>Kerby, R L</au><au>Roberts, G P</au><au>Ludden, P W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Substitution of Valine for Histidine 265 in Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum Affects Activity and Spectroscopic States</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-02-13</date><risdate>1998</risdate><volume>273</volume><issue>7</issue><spage>4059</spage><epage>4064</epage><pages>4059-4064</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><abstract>In carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum , histidine 265 was replaced with valine by site-directed mutagenesis of the cooS gene. The altered form of CODH (H265V) had a low nickel content and a dramatically reduced level of catalytic activity. Although
treatment with NiCl 2 and CoCl 2 increased the activity of H265V CODH by severalfold, activity levels remained more than 1000-fold lower than that of wild-type
CODH. Histidine 265 was not essential for the formation and stability of the Fe 4 S 4 clusters. The K
m and K
D for CO as well as the K
D for cyanide were relatively unchanged as a result of the amino acid substitution in CODH. The time-dependent reduction of
the [Fe 4 S 4 ] 2+ clusters by CO occurred on a time scale of hours, suggesting that, as a consequence of the mutation, a rate-limiting step
had been introduced prior to the transfer of electrons from CO to the cubanes in centers B and C. EPR spectra of H265V CODH
lacked the g av = 1.86 and g av = 1.87 signals characteristic of reduced forms of the active site (center C) of wild-type CODH. This indicates that the electronic
properties of center C have been modified possibly by the disruption or alteration of the ligand-mediated interaction between
the nickel site and Fe 4 S 4 chromophore.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9461598</pmid><doi>10.1074/jbc.273.7.4059</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1998-02, Vol.273 (7), p.4059-4064 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16274640 |
| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Aldehyde Oxidoreductases - chemistry Aldehyde Oxidoreductases - metabolism Binding Sites Carbon Monoxide - metabolism Cobalt - pharmacology Cyanides - metabolism Electron Spin Resonance Spectroscopy Iron - analysis Iron-Sulfur Proteins - genetics Iron-Sulfur Proteins - metabolism Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism Mutagenesis, Site-Directed - genetics Nickel - analysis Nickel - pharmacology Rhodospirillum rubrum - enzymology |
| title | Substitution of Valine for Histidine 265 in Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum Affects Activity and Spectroscopic States |
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