Involvement of sulfhydryl groups in the activation mechanism of the ATPase activity of chloroplast coupling factor 1 [Spinach]
Activation of the ATPase activity and the exposition of a new adenine nucleotide binding site of chloroplast coupling factor 1 (CF1) by dithioerythritol at 25 degrees C were reversed by oxidants. The ATPase activity elicited by heat (63 degrees C, 4 min) was slightly inhibited by oxidants and was pa...
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| Veröffentlicht in: | The Journal of biological chemistry 1982-02, Vol.257 (3), p.1125-1127 |
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| container_title | The Journal of biological chemistry |
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| creator | Arana, J L Vallejos, R H |
| description | Activation of the ATPase activity and the exposition of a new adenine nucleotide binding site of chloroplast coupling factor
1 (CF1) by dithioerythritol at 25 degrees C were reversed by oxidants. The ATPase activity elicited by heat (63 degrees C,
4 min) was slightly inhibited by oxidants and was partially additive with the activity induced by dithioerythritol. Titration
of the thiols of CF1 and determination of their subunit distribution before and after activation by dithioerythritol show
an increase of the free groups from 8 to 10 with the appearance of the 2 new thiols on the gamma subunit. These thiols were
available to reagents in nondenatured enzyme and were reoxidized to a disulfide bond by iodosobenzoate or CuCl2. It is concluded
that the mechanisms of CF1 activation by dithioerythritol and by heat are different and that the former involves a net reduction
of a disulfide bond of the gamma subunit. |
| doi_str_mv | 10.1016/s0021-9258(19)68159-7 |
| format | Article |
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1 (CF1) by dithioerythritol at 25 degrees C were reversed by oxidants. The ATPase activity elicited by heat (63 degrees C,
4 min) was slightly inhibited by oxidants and was partially additive with the activity induced by dithioerythritol. Titration
of the thiols of CF1 and determination of their subunit distribution before and after activation by dithioerythritol show
an increase of the free groups from 8 to 10 with the appearance of the 2 new thiols on the gamma subunit. These thiols were
available to reagents in nondenatured enzyme and were reoxidized to a disulfide bond by iodosobenzoate or CuCl2. It is concluded
that the mechanisms of CF1 activation by dithioerythritol and by heat are different and that the former involves a net reduction
of a disulfide bond of the gamma subunit.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)68159-7</identifier><identifier>PMID: 6460023</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphatases - metabolism ; adenosinetriphosphatase ; chemical modification ; chloroplasts ; Chloroplasts - enzymology ; coupling factor 1 ; Disulfides ; Dithioerythritol - pharmacology ; Enzyme Activation ; Hot Temperature ; Kinetics ; Macromolecular Substances ; Oxidation-Reduction ; Plants - enzymology ; Proton-Translocating ATPases ; sulfhydryl groups</subject><ispartof>The Journal of biological chemistry, 1982-02, Vol.257 (3), p.1125-1127</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4137-4f7e9de5b46863a2c10ae10d71b88af41bf276b65057eeaba49a3db224fb230d3</citedby><cites>FETCH-LOGICAL-c4137-4f7e9de5b46863a2c10ae10d71b88af41bf276b65057eeaba49a3db224fb230d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6460023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arana, J L</creatorcontrib><creatorcontrib>Vallejos, R H</creatorcontrib><creatorcontrib>Escola Superior de Agricultura Luiz de Queiroz, Piracicaba, SP (Brazil)</creatorcontrib><title>Involvement of sulfhydryl groups in the activation mechanism of the ATPase activity of chloroplast coupling factor 1 [Spinach]</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Activation of the ATPase activity and the exposition of a new adenine nucleotide binding site of chloroplast coupling factor
1 (CF1) by dithioerythritol at 25 degrees C were reversed by oxidants. The ATPase activity elicited by heat (63 degrees C,
4 min) was slightly inhibited by oxidants and was partially additive with the activity induced by dithioerythritol. Titration
of the thiols of CF1 and determination of their subunit distribution before and after activation by dithioerythritol show
an increase of the free groups from 8 to 10 with the appearance of the 2 new thiols on the gamma subunit. These thiols were
available to reagents in nondenatured enzyme and were reoxidized to a disulfide bond by iodosobenzoate or CuCl2. It is concluded
that the mechanisms of CF1 activation by dithioerythritol and by heat are different and that the former involves a net reduction
of a disulfide bond of the gamma subunit.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>adenosinetriphosphatase</subject><subject>chemical modification</subject><subject>chloroplasts</subject><subject>Chloroplasts - enzymology</subject><subject>coupling factor 1</subject><subject>Disulfides</subject><subject>Dithioerythritol - pharmacology</subject><subject>Enzyme Activation</subject><subject>Hot Temperature</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Oxidation-Reduction</subject><subject>Plants - enzymology</subject><subject>Proton-Translocating ATPases</subject><subject>sulfhydryl groups</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV2L1DAUhoMo6zj6E1aCF6IX1ZykaZrLZfFjYUFhdkEQCWmaTCNtU5N2ZG787abOsLeemwPnfc4H50XoEsg7IFC9T4RQKCTl9RuQb6sauCzEI7QBUrOCcfj2GG0ekKfoWUo_SY5SwgW6qMoqa2yD_tyMh9Af7GDHGQeH09K77tjGY4_3MSxTwn7Ec2exNrM_6NmHEQ_WdHr0aVgbVu3q7qtOZ8TPx7Vsuj7EMPU6zdjkOb0f99hlIkQM-Ptu8qM23Y_n6InTfbIvznmL7j9-uLv-XNx--XRzfXVbmBKYKEonrGwtb8qqrpimBoi2QFoBTV1rV0LjqKiaihMurNWNLqVmbUNp6RrKSMu26PVp7hTDr8WmWQ0-Gdv3erRhSUowWXEhyH9B4PkgQmUG-Qk0MaQUrVNT9IOORwVErQap3fp9tX5fgVT_DMp7tujyvGBpBts-dJ0dyfqrk975fffbR6saH0xnB0W5UEwBUJ6hlyfI6aD0Pvqk7ncga0Zqzgjh7C9O5aIx</recordid><startdate>19820210</startdate><enddate>19820210</enddate><creator>Arana, J L</creator><creator>Vallejos, R H</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19820210</creationdate><title>Involvement of sulfhydryl groups in the activation mechanism of the ATPase activity of chloroplast coupling factor 1 [Spinach]</title><author>Arana, J L ; Vallejos, R H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4137-4f7e9de5b46863a2c10ae10d71b88af41bf276b65057eeaba49a3db224fb230d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>adenosinetriphosphatase</topic><topic>chemical modification</topic><topic>chloroplasts</topic><topic>Chloroplasts - enzymology</topic><topic>coupling factor 1</topic><topic>Disulfides</topic><topic>Dithioerythritol - pharmacology</topic><topic>Enzyme Activation</topic><topic>Hot Temperature</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Oxidation-Reduction</topic><topic>Plants - enzymology</topic><topic>Proton-Translocating ATPases</topic><topic>sulfhydryl groups</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arana, J L</creatorcontrib><creatorcontrib>Vallejos, R H</creatorcontrib><creatorcontrib>Escola Superior de Agricultura Luiz de Queiroz, Piracicaba, SP (Brazil)</creatorcontrib><collection>AGRIS</collection><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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arana, J L</au><au>Vallejos, R H</au><aucorp>Escola Superior de Agricultura Luiz de Queiroz, Piracicaba, SP (Brazil)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of sulfhydryl groups in the activation mechanism of the ATPase activity of chloroplast coupling factor 1 [Spinach]</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1982-02-10</date><risdate>1982</risdate><volume>257</volume><issue>3</issue><spage>1125</spage><epage>1127</epage><pages>1125-1127</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Activation of the ATPase activity and the exposition of a new adenine nucleotide binding site of chloroplast coupling factor
1 (CF1) by dithioerythritol at 25 degrees C were reversed by oxidants. The ATPase activity elicited by heat (63 degrees C,
4 min) was slightly inhibited by oxidants and was partially additive with the activity induced by dithioerythritol. Titration
of the thiols of CF1 and determination of their subunit distribution before and after activation by dithioerythritol show
an increase of the free groups from 8 to 10 with the appearance of the 2 new thiols on the gamma subunit. These thiols were
available to reagents in nondenatured enzyme and were reoxidized to a disulfide bond by iodosobenzoate or CuCl2. It is concluded
that the mechanisms of CF1 activation by dithioerythritol and by heat are different and that the former involves a net reduction
of a disulfide bond of the gamma subunit.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6460023</pmid><doi>10.1016/s0021-9258(19)68159-7</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1982-02, Vol.257 (3), p.1125-1127 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73965770 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - metabolism adenosinetriphosphatase chemical modification chloroplasts Chloroplasts - enzymology coupling factor 1 Disulfides Dithioerythritol - pharmacology Enzyme Activation Hot Temperature Kinetics Macromolecular Substances Oxidation-Reduction Plants - enzymology Proton-Translocating ATPases sulfhydryl groups |
| title | Involvement of sulfhydryl groups in the activation mechanism of the ATPase activity of chloroplast coupling factor 1 [Spinach] |
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