Measuring the pH dependence of hydrogenase activities
The pH dependences of activities of homogenous hydrogenases of Thiocapsa roseopersicina and Desulfomicrobium baculatum in the reaction of hydrogen uptake in solution in the presence of benzyl viologen and the pH dependences of catalytic currents of hydrogen oxidation by electrodes on which these hyd...
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| Veröffentlicht in: | Biochemistry (Moscow) 2007-09, Vol.72 (9), p.968-973 |
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| container_title | Biochemistry (Moscow) |
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| creator | Tsygankov, A A Minakov, E A Zorin, N A Gosteva, K S Voronin, O G Karyakin, A A |
| description | The pH dependences of activities of homogenous hydrogenases of Thiocapsa roseopersicina and Desulfomicrobium baculatum in the reaction of hydrogen uptake in solution in the presence of benzyl viologen and the pH dependences of catalytic currents of hydrogen oxidation by electrodes on which these hydrogenases were immobilized were compared. Maximal activities of the hydrogenases from T. roseopersicina and D. baculatum in the reaction hydrogen uptake in solution were observed at pH 9.5 and 8.5, respectively. However, the steady-state current caused by catalytic uptake of hydrogen was maximal for the T. roseopersicina hydrogenase-containing electrode at pH 5.5-6.5 under overvoltage of 30-60 mV, whereas for electrodes with D. baculatum hydrogenase it was maximal at pH 6.0-6.5. Analysis of these data suggests that pH-dependent changes in the hydrogenase activities in solution during hydrogen uptake are due not only to the effect of proton concentration on the enzyme conformation or protonation of certain groups of the enzyme active center, but they are rather indicative of changes in free energy of the reaction accompanying changes in pH. |
| doi_str_mv | 10.1134/s0006297907090076 |
| format | Article |
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Maximal activities of the hydrogenases from T. roseopersicina and D. baculatum in the reaction hydrogen uptake in solution were observed at pH 9.5 and 8.5, respectively. However, the steady-state current caused by catalytic uptake of hydrogen was maximal for the T. roseopersicina hydrogenase-containing electrode at pH 5.5-6.5 under overvoltage of 30-60 mV, whereas for electrodes with D. baculatum hydrogenase it was maximal at pH 6.0-6.5. Analysis of these data suggests that pH-dependent changes in the hydrogenase activities in solution during hydrogen uptake are due not only to the effect of proton concentration on the enzyme conformation or protonation of certain groups of the enzyme active center, but they are rather indicative of changes in free energy of the reaction accompanying changes in pH.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/s0006297907090076</identifier><identifier>PMID: 17922655</identifier><language>eng</language><publisher>United States: Springer</publisher><subject>Bacteria ; Benzyl Viologen - chemistry ; Binding Sites ; Desulfovibrio - enzymology ; Electrodes ; Enzymes ; Hydrogen ; Hydrogen - chemistry ; Hydrogen-Ion Concentration ; Hydrogenase - metabolism ; Hydrogenases ; Influence ; Observations ; Properties ; Temperature effects ; Thiocapsa roseopersicina - enzymology</subject><ispartof>Biochemistry (Moscow), 2007-09, Vol.72 (9), p.968-973</ispartof><rights>COPYRIGHT 2007 Springer</rights><rights>Nauka/Interperiodica 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-db8196c76a8b9fec2e6383e816fced036a7ce6c34e48a82cda86a9329b92c5223</citedby><cites>FETCH-LOGICAL-c420t-db8196c76a8b9fec2e6383e816fced036a7ce6c34e48a82cda86a9329b92c5223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17922655$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsygankov, A A</creatorcontrib><creatorcontrib>Minakov, E A</creatorcontrib><creatorcontrib>Zorin, N A</creatorcontrib><creatorcontrib>Gosteva, K S</creatorcontrib><creatorcontrib>Voronin, O G</creatorcontrib><creatorcontrib>Karyakin, A A</creatorcontrib><title>Measuring the pH dependence of hydrogenase activities</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry (Mosc)</addtitle><description>The pH dependences of activities of homogenous hydrogenases of Thiocapsa roseopersicina and Desulfomicrobium baculatum in the reaction of hydrogen uptake in solution in the presence of benzyl viologen and the pH dependences of catalytic currents of hydrogen oxidation by electrodes on which these hydrogenases were immobilized were compared. Maximal activities of the hydrogenases from T. roseopersicina and D. baculatum in the reaction hydrogen uptake in solution were observed at pH 9.5 and 8.5, respectively. However, the steady-state current caused by catalytic uptake of hydrogen was maximal for the T. roseopersicina hydrogenase-containing electrode at pH 5.5-6.5 under overvoltage of 30-60 mV, whereas for electrodes with D. baculatum hydrogenase it was maximal at pH 6.0-6.5. Analysis of these data suggests that pH-dependent changes in the hydrogenase activities in solution during hydrogen uptake are due not only to the effect of proton concentration on the enzyme conformation or protonation of certain groups of the enzyme active center, but they are rather indicative of changes in free energy of the reaction accompanying changes in pH.</description><subject>Bacteria</subject><subject>Benzyl Viologen - chemistry</subject><subject>Binding Sites</subject><subject>Desulfovibrio - enzymology</subject><subject>Electrodes</subject><subject>Enzymes</subject><subject>Hydrogen</subject><subject>Hydrogen - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrogenase - metabolism</subject><subject>Hydrogenases</subject><subject>Influence</subject><subject>Observations</subject><subject>Properties</subject><subject>Temperature effects</subject><subject>Thiocapsa roseopersicina - enzymology</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNpdkE9Lw0AQxRdRbK1-AC8SFLxFZ_9ks3ssRa1Q8aCel81m0qakSdxNhH57E1oQPA3D-703wyPkmsIDpVw8BgCQTKcaUtAAqTwhUypBxRwEnJLpKMejPiEXIWyHlYHm52RCU82YTJIpSd7Qht6X9TrqNhi1yyjHFusca4dRU0Sbfe6bNdY2YGRdV_6UXYnhkpwVtgp4dZwz8vX89LlYxqv3l9fFfBU7waCL80xRLV0qrcp0gY6h5IqjorJwmAOXNnUoHRcolFXM5VZJqznTmWYuYYzPyP0ht_XNd4-hM7syOKwqW2PTByMVl0xwPYC3_8Bt0_t6-M2kVHMBmtEBujtAa1uhKeui6bx1Y6KZU6mlTlIBA0UPlPNNCB4L0_pyZ_3eUDBj7ebjf-2D5-Z4vs92mP85jj3zX65YeqQ</recordid><startdate>20070901</startdate><enddate>20070901</enddate><creator>Tsygankov, A A</creator><creator>Minakov, E A</creator><creator>Zorin, N A</creator><creator>Gosteva, K S</creator><creator>Voronin, O G</creator><creator>Karyakin, A A</creator><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20070901</creationdate><title>Measuring the pH dependence of hydrogenase activities</title><author>Tsygankov, A A ; 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Maximal activities of the hydrogenases from T. roseopersicina and D. baculatum in the reaction hydrogen uptake in solution were observed at pH 9.5 and 8.5, respectively. However, the steady-state current caused by catalytic uptake of hydrogen was maximal for the T. roseopersicina hydrogenase-containing electrode at pH 5.5-6.5 under overvoltage of 30-60 mV, whereas for electrodes with D. baculatum hydrogenase it was maximal at pH 6.0-6.5. Analysis of these data suggests that pH-dependent changes in the hydrogenase activities in solution during hydrogen uptake are due not only to the effect of proton concentration on the enzyme conformation or protonation of certain groups of the enzyme active center, but they are rather indicative of changes in free energy of the reaction accompanying changes in pH.</abstract><cop>United States</cop><pub>Springer</pub><pmid>17922655</pmid><doi>10.1134/s0006297907090076</doi><tpages>6</tpages></addata></record> |
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| subjects | Bacteria Benzyl Viologen - chemistry Binding Sites Desulfovibrio - enzymology Electrodes Enzymes Hydrogen Hydrogen - chemistry Hydrogen-Ion Concentration Hydrogenase - metabolism Hydrogenases Influence Observations Properties Temperature effects Thiocapsa roseopersicina - enzymology |
| title | Measuring the pH dependence of hydrogenase activities |
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