書誌事項
- タイトル別名
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- The Analysis of Chemical Reaction on Adenosinetriphosphate Synthase by Recombinant Deoxyribonucleic Acid Method
- 遺伝子組換えによるアデノシン3リン酸合成酵素の化学反応の解析
- イデンシ クミカエ ニ ヨル アデノシン 3 リンサン ゴウセイ コウソ ノ
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Adenosinetriphosphate (ATP) synthase (FoF1) is a major energy supplying enzyme of cells utilizing the proton motive force. It consists of a catalytic portion called F1 and a proton channel portion called Fo. In order to elucidate the chemical reaction of FoF1, thermophilic FoF1 (TFoF1) was used, because it is stable and could eb reconstituted without Mg-ATP. In contrast to the previous hypotheses on the ATP synthesis, direct measurement of H+ current through TFoF1 incorporated into a planar lipid bilayer, 3H+/ATP stoichiometry was obtained. The primary structure of TFoF1 was established by sequencing its operon deoxyribonucleic acid and subunit peptides. The stereochemistry of the reaction using [16O, 17O, 15O, 35S] thiophosphate supported the a pathway for associative nucleophilic displacement on a phosphoric ester without pseudorotation. The diastereoisomeric preference of Cd-ATPγS revealed that the true substrate of TFoF1 is Δ, β, γ, bidentate Mg-ATP, like adenylate kinase. The site directed mutagenesis of the residues of F1 homologous to Mg-ATP binding site of adenylate kinase revealed their essential role in the reaction. Mitchell's chemiosmotic theory was refined by these results.
収録刊行物
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- 薬学雑誌
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薬学雑誌 107 (11), 835-848, 1987
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390282681132164224
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- NII論文ID
- 110003649716
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- NII書誌ID
- AN00284903
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- ISSN
- 13475231
- 00316903
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- NDL書誌ID
- 3158422
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- データソース種別
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- JaLC
- NDL
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