{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T11:21:12Z","timestamp":1758280872705},"reference-count":36,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2008,6,28]],"date-time":"2008-06-28T00:00:00Z","timestamp":1214611200000},"content-version":"vor","delay-in-days":10590,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1979,7]]},"abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>A large series of 3\u2032 esters of ADP has been synthesized. Several of these can serve as photoaffinity labels; others exhibit fluorescent properties. The corresponding AMP and ATP derivatives have also been synthesized in some cases.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The influence of the 3\u2032\u2010<jats:italic>O<\/jats:italic>\u2010acyl nucleotides on energy\u2010linked functions of beef\u2010heart submitochondrial particles has been investigated. The following results were obtained.<\/jats:p><jats:p>a) 3\u2032 Esters of ADP are powerful and highly specific inhibitors of oxidative phosphorylation. The inhibition is competitive to ADP and <jats:italic>K<\/jats:italic><jats:sub>i<\/jats:sub> values as low as 0.05 \u03bcM, for the 3\u2032\u2010<jats:italic>O<\/jats:italic>\u2010(1)naphthoyl ester of ADP, could be observed.<\/jats:p><jats:p>b) The inhibition of oxidative phosphorylation by 3\u2032 esters of ADP appears to be non\u2010competitive versus inorganic phosphate.<\/jats:p><jats:p>c) The nucleotide analogs are not phosphorylated themselves. The corresponding ATP analogs can not drive energy\u2010linked processes.<\/jats:p><jats:p>d) The 3\u2032 esters of AMP are ineffective as inhibitors, whereas the ATP derivatives are only comparatively weak inhibitors.<\/jats:p><jats:p>e) Uncoupled or solubilized ATPase is almost two orders of magnitude less sensitive against inhibition by 3\u2032 esters than coupled systems. The analogs exert maximal inhibition specifically in systems involving an \u2018energized\u2019 state of the coupling device.<\/jats:p><jats:p>f) Azido\u2010group\u2010bearing analogs can be used for irreversible photoinactivation of the coupling ATPase. Photoinactivation also is most efficient when carried out with \u2018energized\u2019 particles.<\/jats:p><jats:p>g) The inhibitory properties are similar also in ATP\u2010driven NAD<jats:sup>+<\/jats:sup> reduction by succinate, and in the uncoupler\u2010sensitive ATP \u21cc P<jats:sub>i<\/jats:sub> exchange. The required concentrations for half\u2010maximal inhibition are somewhat higher than in oxidative phosphorylation, but lower than with uncoupled ATPase.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>From molecular models, from substituent properties, and from the conditions required for inhibition it is concluded that these highly effective analogs of ADP may act as conformation\u2010specific probes at the catalytic site of oxidative phosphorylation. The results are interpreted in terms of a model suggesting that, in the process of ATP synthesis, a hydrophobic cavity on the enzyme is exposed only in the energized state, accepting the large 3\u2032 substituent. The substituent is assumed to inhibit phosphoryl transfer and\/or conformational transitions inherent in the process of ADP phosphorylation by steric hinderance.<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p>","DOI":"10.1111\/j.1432-1033.1979.tb13129.x","type":"journal-article","created":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T19:58:56Z","timestamp":1109879936000},"page":"415-424","source":"Crossref","is-referenced-by-count":27,"title":["3\u2032 Esters of ADP as Energy\u2010Transfer Inhibitors and Probes of the Catalytic Site of Oxidative Phosphorylation"],"prefix":"10.1111","volume":"97","author":[{"given":"G\u00fcnter","family":"SCH\u00c4FER","sequence":"first","affiliation":[]},{"given":"G\u00fcnes","family":"ONUR","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,6,28]]},"reference":[{"key":"e_1_2_3_2_2","doi-asserted-by":"publisher","DOI":"10.1002\/jss.400030303"},{"key":"e_1_2_3_3_2","doi-asserted-by":"publisher","DOI":"10.1002\/jss.400030304"},{"key":"e_1_2_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)42612-4"},{"key":"e_1_2_3_5_2","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/S0021-9258(17)32733-3","volume":"252","author":"Schuster S. M.","year":"1976","journal-title":"J. Biol. Chem."},{"key":"e_1_2_3_6_2","first-page":"319","volume-title":"Structure and Function of Energy Transducing Membranes","author":"Harris D. A.","year":"1977"},{"key":"e_1_2_3_7_2","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/0005-2728(77)90147-5","volume":"460","author":"Wagenvoord R. J.","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"e_1_2_3_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1978.tb12445.x"},{"key":"e_1_2_3_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(76)91033-0"},{"key":"e_1_2_3_10_2","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0014-5793(77)80466-3","volume":"80","author":"Lunadri J.","year":"1977","journal-title":"FEBS Lett."},{"key":"e_1_2_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)40893-4"},{"key":"e_1_2_3_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(75)90365-4"},{"key":"e_1_2_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0304-4173(78)90002-2"},{"key":"e_1_2_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(77)90054-8"},{"key":"e_1_2_3_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(78)80360-3"},{"key":"e_1_2_3_16_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-81287-3_17"},{"key":"e_1_2_3_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(67)10015-3"},{"key":"e_1_2_3_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(67)10037-2"},{"key":"e_1_2_3_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(74)32024-1"},{"key":"e_1_2_3_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(67)10012-8"},{"key":"e_1_2_3_21_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)40483-2"},{"key":"e_1_2_3_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(67)10120-1"},{"key":"e_1_2_3_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0040-4020(01)93090-X"},{"key":"e_1_2_3_24_2","doi-asserted-by":"publisher","DOI":"10.1002\/cber.188001302111"},{"key":"e_1_2_3_25_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj1280499"},{"key":"e_1_2_3_26_2","unstructured":"Reference deleted."},{"key":"e_1_2_3_27_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00675a010"},{"key":"e_1_2_3_28_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj0850257"},{"key":"e_1_2_3_29_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00896a020"},{"key":"e_1_2_3_30_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00883a032"},{"key":"e_1_2_3_31_2","first-page":"295","volume-title":"Structure and Function of Energy Transducing Membranes","author":"Kasahara M.","year":"1977"},{"key":"e_1_2_3_32_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(76)80252-5"},{"key":"e_1_2_3_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)40484-4"},{"key":"e_1_2_3_34_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(78)90091-9"},{"key":"e_1_2_3_35_2","first-page":"994","volume-title":"Oxygenases and Related Redox Systems","author":"Boyer P. D.","year":"1965"},{"key":"e_1_2_3_36_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-81287-3_20"},{"key":"e_1_2_3_37_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1975.tb04120.x"}],"container-title":["European Journal of Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1111%2Fj.1432-1033.1979.tb13129.x","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/j.1432-1033.1979.tb13129.x","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,23]],"date-time":"2023-11-23T17:53:05Z","timestamp":1700761985000},"score":1,"resource":{"primary":{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/10.1111\/j.1432-1033.1979.tb13129.x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,7]]},"references-count":36,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1979,7]]}},"alternative-id":["10.1111\/j.1432-1033.1979.tb13129.x"],"URL":"https:\/\/doi.org\/10.1111\/j.1432-1033.1979.tb13129.x","archive":["Portico"],"relation":{},"ISSN":["0014-2956","1432-1033"],"issn-type":[{"value":"0014-2956","type":"print"},{"value":"1432-1033","type":"electronic"}],"subject":[],"published":{"date-parts":[[1979,7]]}}}