Photoaffinity cross‐linking of F1ATPase from spinach chloroplasts by 3'‐arylazido‐β‐alanyl‐8‐azido ATP

FEBS Letters

Berzborn, Richard J.²  Rathgeber, Gabriele¹  Schuhen, Achim¹  Schäfer, Hans-Jochen¹ 

[1] Institut für Biochemie, Johannes Gutenberg-Universität, Becherweg 30, D-55099 Mainz, Germany;Lehrstuhl für Biochemie der Pflanzen, Ruhr-Universität, D-44780 Bochum, Germany

关键词: F1ATPase;    Chloroplast;    Photoaffinity cross-linking;    Interfacial localization;    Nucleotide binding site;    CF1;    coupling factor 1 (ATPase) from chloroplasts;    F1;    F1ATPase from mitochondria or bacteria;    F0F1;    F0F1ATPase;    ATP synthase;    2;    3'-DIN3ATP;    3'-O-{3-[N-(4-azido-2-nitrophenyl)amino]-propionyl}2-azidoadenosine 5-triphosphate;    8;    3'-DiN3ATP;    3'-aryl-azido-β-alanyl-8-azido ATP;    3'-O-{3-[N-(4-azido-2-nitrophenyl)amino]propionyl}8-azidoadenosine 5-triphosphate;    FSB-8-N3A;    5'-p-fluorosulfonylbenzoyl-8-azidoadenosine;    TNP-ATP;    2';    3'-O-(2;    4;    6-trinitrophenyl)-adenosine 5'-triphosphate;   

DOI  :  10.1016/0014-5793(94)80151-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

UV irradiation of the ATPase (CF₁) from spinach chloroplasts in the presence of 3'-arylazido-β-alanyl-8-azido ATP (8,3'-DiN₃ATP) results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of α-β cross-links. The results demonstrate an interfacial localization of the nucleotide binding sites on CF₁.

【 授权许可】

Unknown