Kinetics and energetics of redox regulation of ATP synthase from chloroplasts
The rate of ATP hydrolysis catalyzed by the membrane-bound CF 0F 1 ATP synthase from chloroplasts served as a probe for the determination of the reduction grade of the enzyme treated with dithiothreitol (DTT) or thioredoxin. Rate constants for reduction were obtained. It turns out that reduction by...
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| Veröffentlicht in: | FEBS letters 1993-05, Vol.323 (1), p.19-22 |
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| creator | Strelow, Frank Rumberg, Bernd |
| description | The rate of ATP hydrolysis catalyzed by the membrane-bound CF
0F
1 ATP synthase from chloroplasts served as a probe for the determination of the reduction grade of the enzyme treated with dithiothreitol (DTT) or thioredoxin. Rate constants for reduction were obtained. It turns out that reduction by thioredoxin is about a factor of 6,000 more effective than DTT reduction. The activation profiles with respect to ΔpH were obtained for reduced and oxidized ATPases. The activation curve of reduced enzyme turns out to have its half-maximum degree of activation at ΔPH = 1.65, which is considerably lower than reported hitherto. The corresponding value of the oxidized enzyme has been obtained from the rate of ATP hydrolysis in the case of incomplete reduced ATPases, taking into account the aforementioned rate constants, and comes to ΔpH = 3.35. |
| doi_str_mv | 10.1016/0014-5793(93)81439-7 |
| format | Article |
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0F
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0F
1 ATP synthase from chloroplasts served as a probe for the determination of the reduction grade of the enzyme treated with dithiothreitol (DTT) or thioredoxin. Rate constants for reduction were obtained. It turns out that reduction by thioredoxin is about a factor of 6,000 more effective than DTT reduction. The activation profiles with respect to ΔpH were obtained for reduced and oxidized ATPases. The activation curve of reduced enzyme turns out to have its half-maximum degree of activation at ΔPH = 1.65, which is considerably lower than reported hitherto. The corresponding value of the oxidized enzyme has been obtained from the rate of ATP hydrolysis in the case of incomplete reduced ATPases, taking into account the aforementioned rate constants, and comes to ΔpH = 3.35.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ATP synthase</subject><subject>Biological and medical sciences</subject><subject>Chloroplast</subject><subject>Chloroplasts - enzymology</subject><subject>Enzyme Activation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>Kinetics</subject><subject>Latent ATPase</subject><subject>Oxidation-Reduction</subject><subject>Plants</subject><subject>Sulfhydryl Compounds - metabolism</subject><subject>Thermodynamics</subject><subject>Thiol regulation</subject><subject>Thioredoxin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUE1P3DAUtFDRdvn4B62UQ4XgELBjO7YvSIBYQIDoYXu2vM4LuMrGi50A--9xyGqPVSXL1ps3b_xmEPpB8CnBpDzDmLCcC0WPFT2RhFGVix00JVLQnLJSfkPTLeU72ovxL061JGqCJpIpLqiaosd710LnbMxMW2XQQngeS19nASr_ke7nvjGd8-2AXcx_Z3Hddi8mQlYHv8zsS-ODXzUmdvEA7damiXC4effRn9n1_Oo2f3i6ubu6eMgtY0rklKgCpCFQFMrWwJnBace6WGDO-UIqpgyvSsOtKkEkZ6wQlFW2qvmCSJn87aOjUXcV_GsPsdNLFy00jWnB91ELLlhBFU5ENhJt8DEGqPUquKUJa02wHlLUQ0R6iEin85WiHvR_bvT7xRKq7dAmttT_tembaE1TB9NaF7c0JgSRZZFos5H27hpY_9fXenZ9WQyNAVf0Cx32OR-FIIX65iDoaB20FioXwHa68u7fhj4BF_WgWQ</recordid><startdate>19930524</startdate><enddate>19930524</enddate><creator>Strelow, Frank</creator><creator>Rumberg, Bernd</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7X8</scope></search><sort><creationdate>19930524</creationdate><title>Kinetics and energetics of redox regulation of ATP synthase from chloroplasts</title><author>Strelow, Frank ; Rumberg, Bernd</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4497-3192e8a1e229cfe54a0793f2b0555b8949a5d6a5c96e781442734dcdf5b188873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ATP synthase</topic><topic>Biological and medical sciences</topic><topic>Chloroplast</topic><topic>Chloroplasts - enzymology</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases</topic><topic>Kinetics</topic><topic>Latent ATPase</topic><topic>Oxidation-Reduction</topic><topic>Plants</topic><topic>Sulfhydryl Compounds - metabolism</topic><topic>Thermodynamics</topic><topic>Thiol regulation</topic><topic>Thioredoxin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Strelow, Frank</creatorcontrib><creatorcontrib>Rumberg, Bernd</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Strelow, Frank</au><au>Rumberg, Bernd</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics and energetics of redox regulation of ATP synthase from chloroplasts</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1993-05-24</date><risdate>1993</risdate><volume>323</volume><issue>1</issue><spage>19</spage><epage>22</epage><pages>19-22</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The rate of ATP hydrolysis catalyzed by the membrane-bound CF
0F
1 ATP synthase from chloroplasts served as a probe for the determination of the reduction grade of the enzyme treated with dithiothreitol (DTT) or thioredoxin. Rate constants for reduction were obtained. It turns out that reduction by thioredoxin is about a factor of 6,000 more effective than DTT reduction. The activation profiles with respect to ΔpH were obtained for reduced and oxidized ATPases. The activation curve of reduced enzyme turns out to have its half-maximum degree of activation at ΔPH = 1.65, which is considerably lower than reported hitherto. The corresponding value of the oxidized enzyme has been obtained from the rate of ATP hydrolysis in the case of incomplete reduced ATPases, taking into account the aforementioned rate constants, and comes to ΔpH = 3.35.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>8495739</pmid><doi>10.1016/0014-5793(93)81439-7</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1993-05, Vol.323 (1), p.19-22 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - metabolism Analytical, structural and metabolic biochemistry ATP synthase Biological and medical sciences Chloroplast Chloroplasts - enzymology Enzyme Activation Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases Kinetics Latent ATPase Oxidation-Reduction Plants Sulfhydryl Compounds - metabolism Thermodynamics Thiol regulation Thioredoxin |
| title | Kinetics and energetics of redox regulation of ATP synthase from chloroplasts |
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