Effect of pH on the mitochondrial energy-linked and non-energy-linked transhydrogenation reactions
The effect of pH on the kinetics of the following transhydrogenation reactions catalyzed by energized and nonenergized submitochondrial particles has been studied: NADH leads to 3-acetylpyridine adenine dinucleotide phosphate (AcPyADP), NADH leads to thionicotinamide adenine dinucleotide phosphate (...
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| Veröffentlicht in: | The Journal of biological chemistry 1980-10, Vol.255 (20), p.9641-9646 |
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| creator | Galante, Y M Lee, Y Hatefi, Y |
| description | The effect of pH on the kinetics of the following transhydrogenation reactions catalyzed by energized and nonenergized submitochondrial
particles has been studied: NADH leads to 3-acetylpyridine adenine dinucleotide phosphate (AcPyADP), NADH leads to thionicotinamide
adenine dinucleotide phosphate (thioNADP), NADPH leads to AcPyADP, and NADPH leads to thioNADP. The effect of membrane energization
on reaction rates can be approximated in the case of NADH leads to AcPyADP and thioNADP transhydrogenations, or equaled in
the case of NADPH leads to AcPyADP and thioNADP transhydrogenations by lowering the assay pH to less than or equal to 6.0.
For the reactions NADH leads to AcPyADP and thioNADP under energy-linked conditions, substrate Km values are lowest and Vmax
values are highest at pH 7 to 7.5, the optimum pH for mitochondrial energy transduction processes. Under non-energy-linked
conditions, however, Km values were lowest and Vmax values were highest at the most acid conditions (pH = 5.5) examined. Plots
of ln (Vmax/Km) (an index of enzyme-substrate affinity to form a complex) versus pH showed the highest affinity at pH 7 to
7.5 for energy-linked conditions. Similar plots for non-energy-linked conditions. Similar plots for non-energy-linked conditions.
Similar plots for non-energy-linked conditions showed a sharp and linear increase in the value of ln (Vmax/Km) as the assay
pH was lowered from 8.5 to 6 to 6.5. This was followed by a less steep line down to pH 5.5, with a clear break at pH 6 to
6.5. These results suggested the involvement of ionizable group(s) with pK value(s) at pH 6 to 6.5 affecting enzyme-substrate
binding under non-energy-linked conditions. An analogous mechanism, possibly by way of proton-induced conformation change
of the transhydrogenase enzyme (EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the
rate of transhydrogenation under energy-linked conditions.roton-induced conformation change of the transhydrogenase enzyme
(EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the rate of transhydrogenation under
energy-linked conditions. |
| doi_str_mv | 10.1016/S0021-9258(18)43440-0 |
| format | Article |
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particles has been studied: NADH leads to 3-acetylpyridine adenine dinucleotide phosphate (AcPyADP), NADH leads to thionicotinamide
adenine dinucleotide phosphate (thioNADP), NADPH leads to AcPyADP, and NADPH leads to thioNADP. The effect of membrane energization
on reaction rates can be approximated in the case of NADH leads to AcPyADP and thioNADP transhydrogenations, or equaled in
the case of NADPH leads to AcPyADP and thioNADP transhydrogenations by lowering the assay pH to less than or equal to 6.0.
For the reactions NADH leads to AcPyADP and thioNADP under energy-linked conditions, substrate Km values are lowest and Vmax
values are highest at pH 7 to 7.5, the optimum pH for mitochondrial energy transduction processes. Under non-energy-linked
conditions, however, Km values were lowest and Vmax values were highest at the most acid conditions (pH = 5.5) examined. Plots
of ln (Vmax/Km) (an index of enzyme-substrate affinity to form a complex) versus pH showed the highest affinity at pH 7 to
7.5 for energy-linked conditions. Similar plots for non-energy-linked conditions. Similar plots for non-energy-linked conditions.
Similar plots for non-energy-linked conditions showed a sharp and linear increase in the value of ln (Vmax/Km) as the assay
pH was lowered from 8.5 to 6 to 6.5. This was followed by a less steep line down to pH 5.5, with a clear break at pH 6 to
6.5. These results suggested the involvement of ionizable group(s) with pK value(s) at pH 6 to 6.5 affecting enzyme-substrate
binding under non-energy-linked conditions. An analogous mechanism, possibly by way of proton-induced conformation change
of the transhydrogenase enzyme (EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the
rate of transhydrogenation under energy-linked conditions.roton-induced conformation change of the transhydrogenase enzyme
(EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the rate of transhydrogenation under
energy-linked conditions.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)43440-0</identifier><identifier>PMID: 7430091</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Cattle ; Hydrogen-Ion Concentration ; Kinetics ; Mitochondria - metabolism ; Mitochondria, Heart - metabolism ; NAD - analogs & derivatives ; NAD - metabolism ; NADH, NADPH Oxidoreductases - metabolism ; NADP - analogs & derivatives ; NADP - metabolism ; NADP Transhydrogenases - metabolism ; Oxidation-Reduction ; Structure-Activity Relationship ; Submitochondrial Particles - metabolism</subject><ispartof>The Journal of biological chemistry, 1980-10, Vol.255 (20), p.9641-9646</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-517bdf5bea29bf31db88d34882f8d24dd39713938bdde9da05db8606d34a05f23</citedby><cites>FETCH-LOGICAL-c379t-517bdf5bea29bf31db88d34882f8d24dd39713938bdde9da05db8606d34a05f23</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/7430091$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Galante, Y M</creatorcontrib><creatorcontrib>Lee, Y</creatorcontrib><creatorcontrib>Hatefi, Y</creatorcontrib><title>Effect of pH on the mitochondrial energy-linked and non-energy-linked transhydrogenation reactions</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The effect of pH on the kinetics of the following transhydrogenation reactions catalyzed by energized and nonenergized submitochondrial
particles has been studied: NADH leads to 3-acetylpyridine adenine dinucleotide phosphate (AcPyADP), NADH leads to thionicotinamide
adenine dinucleotide phosphate (thioNADP), NADPH leads to AcPyADP, and NADPH leads to thioNADP. The effect of membrane energization
on reaction rates can be approximated in the case of NADH leads to AcPyADP and thioNADP transhydrogenations, or equaled in
the case of NADPH leads to AcPyADP and thioNADP transhydrogenations by lowering the assay pH to less than or equal to 6.0.
For the reactions NADH leads to AcPyADP and thioNADP under energy-linked conditions, substrate Km values are lowest and Vmax
values are highest at pH 7 to 7.5, the optimum pH for mitochondrial energy transduction processes. Under non-energy-linked
conditions, however, Km values were lowest and Vmax values were highest at the most acid conditions (pH = 5.5) examined. Plots
of ln (Vmax/Km) (an index of enzyme-substrate affinity to form a complex) versus pH showed the highest affinity at pH 7 to
7.5 for energy-linked conditions. Similar plots for non-energy-linked conditions. Similar plots for non-energy-linked conditions.
Similar plots for non-energy-linked conditions showed a sharp and linear increase in the value of ln (Vmax/Km) as the assay
pH was lowered from 8.5 to 6 to 6.5. This was followed by a less steep line down to pH 5.5, with a clear break at pH 6 to
6.5. These results suggested the involvement of ionizable group(s) with pK value(s) at pH 6 to 6.5 affecting enzyme-substrate
binding under non-energy-linked conditions. An analogous mechanism, possibly by way of proton-induced conformation change
of the transhydrogenase enzyme (EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the
rate of transhydrogenation under energy-linked conditions.roton-induced conformation change of the transhydrogenase enzyme
(EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the rate of transhydrogenation under
energy-linked conditions.</description><subject>Animals</subject><subject>Cattle</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria, Heart - metabolism</subject><subject>NAD - analogs & derivatives</subject><subject>NAD - metabolism</subject><subject>NADH, NADPH Oxidoreductases - metabolism</subject><subject>NADP - analogs & derivatives</subject><subject>NADP - metabolism</subject><subject>NADP Transhydrogenases - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Structure-Activity Relationship</subject><subject>Submitochondrial Particles - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtLxDAQgIMouj5-glAQRA_VpEm2yVEWXyB4UMFbSJvJNtoma9JF9t-bdRfBucww880MfAidEnxFMJlev2BckVJWXFwQcckoY7jEO2hCsKAl5eR9F03-kAN0mNIHzsEk2Uf7NaMYSzJBza210I5FsMXioQi-GDsoBjeGtgveRKf7AjzE-arsnf8EU2hvCh98-b87Ru1TtzIxzMHr0eVDEXS7LtIx2rO6T3CyzUfo7e72dfZQPj3fP85unsqW1nIsOakbY3kDupKNpcQ0QhjKhKisMBUzhsqaUElFYwxIozHPxBRPM5NrW9EjdL65u4jhawlpVINLLfS99hCWSdWcUkYFySDfgG0MKUWwahHdoONKEazWbtWvW7UWp4hQv24Vznun2wfLZgDzt7WVmednm3nn5t23i6Aalz3CoCrOVYWVnDJCfwDxw4H0</recordid><startdate>19801025</startdate><enddate>19801025</enddate><creator>Galante, Y M</creator><creator>Lee, Y</creator><creator>Hatefi, Y</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>7X8</scope></search><sort><creationdate>19801025</creationdate><title>Effect of pH on the mitochondrial energy-linked and non-energy-linked transhydrogenation reactions</title><author>Galante, Y M ; Lee, Y ; Hatefi, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-517bdf5bea29bf31db88d34882f8d24dd39713938bdde9da05db8606d34a05f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondria, Heart - metabolism</topic><topic>NAD - analogs & derivatives</topic><topic>NAD - metabolism</topic><topic>NADH, NADPH Oxidoreductases - metabolism</topic><topic>NADP - analogs & derivatives</topic><topic>NADP - metabolism</topic><topic>NADP Transhydrogenases - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Structure-Activity Relationship</topic><topic>Submitochondrial Particles - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Galante, Y M</creatorcontrib><creatorcontrib>Lee, Y</creatorcontrib><creatorcontrib>Hatefi, Y</creatorcontrib><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Galante, Y M</au><au>Lee, Y</au><au>Hatefi, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of pH on the mitochondrial energy-linked and non-energy-linked transhydrogenation reactions</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1980-10-25</date><risdate>1980</risdate><volume>255</volume><issue>20</issue><spage>9641</spage><epage>9646</epage><pages>9641-9646</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The effect of pH on the kinetics of the following transhydrogenation reactions catalyzed by energized and nonenergized submitochondrial
particles has been studied: NADH leads to 3-acetylpyridine adenine dinucleotide phosphate (AcPyADP), NADH leads to thionicotinamide
adenine dinucleotide phosphate (thioNADP), NADPH leads to AcPyADP, and NADPH leads to thioNADP. The effect of membrane energization
on reaction rates can be approximated in the case of NADH leads to AcPyADP and thioNADP transhydrogenations, or equaled in
the case of NADPH leads to AcPyADP and thioNADP transhydrogenations by lowering the assay pH to less than or equal to 6.0.
For the reactions NADH leads to AcPyADP and thioNADP under energy-linked conditions, substrate Km values are lowest and Vmax
values are highest at pH 7 to 7.5, the optimum pH for mitochondrial energy transduction processes. Under non-energy-linked
conditions, however, Km values were lowest and Vmax values were highest at the most acid conditions (pH = 5.5) examined. Plots
of ln (Vmax/Km) (an index of enzyme-substrate affinity to form a complex) versus pH showed the highest affinity at pH 7 to
7.5 for energy-linked conditions. Similar plots for non-energy-linked conditions. Similar plots for non-energy-linked conditions.
Similar plots for non-energy-linked conditions showed a sharp and linear increase in the value of ln (Vmax/Km) as the assay
pH was lowered from 8.5 to 6 to 6.5. This was followed by a less steep line down to pH 5.5, with a clear break at pH 6 to
6.5. These results suggested the involvement of ionizable group(s) with pK value(s) at pH 6 to 6.5 affecting enzyme-substrate
binding under non-energy-linked conditions. An analogous mechanism, possibly by way of proton-induced conformation change
of the transhydrogenase enzyme (EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the
rate of transhydrogenation under energy-linked conditions.roton-induced conformation change of the transhydrogenase enzyme
(EC 1.6.1.1), might be involved in increasing enzyme-substrate affinity and consequently the rate of transhydrogenation under
energy-linked conditions.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7430091</pmid><doi>10.1016/S0021-9258(18)43440-0</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1980-10, Vol.255 (20), p.9641-9646 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75334381 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Cattle Hydrogen-Ion Concentration Kinetics Mitochondria - metabolism Mitochondria, Heart - metabolism NAD - analogs & derivatives NAD - metabolism NADH, NADPH Oxidoreductases - metabolism NADP - analogs & derivatives NADP - metabolism NADP Transhydrogenases - metabolism Oxidation-Reduction Structure-Activity Relationship Submitochondrial Particles - metabolism |
| title | Effect of pH on the mitochondrial energy-linked and non-energy-linked transhydrogenation reactions |
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