Matsuno-Yagi A, Yagi T, Hatefi Y
Proc Natl Acad Sci U S A. 1985 Nov;82(22):7550-4. doi: 10.1073/pnas.82.22.7550.
Aurovertin is a fluorescent antibiotic that binds to the catalytic beta subunits of the mitochondrial F1-ATPase and inhibits ATP synthesis and hydrolysis. ATP, ADP, and membrane energization in submitochondrial particles (SMP) alter the fluorescence of F1-bound aurovertin. These fluorescence changes are considered to be in response to the conformation changes of F1-ATPase. This paper shows that the ATP-induced fluorescence change of aurovertin bound to SMP or complex V (purified ATP synthase complex F0-F1) is inhibited when these preparations are pretreated with oligomycin or N,N'-dicyclohexylcarbodiimide (DCCD). This inhibition is not seen with isolated F1-ATPase. These and other results have suggested that modifications of the DCCD-binding protein in the membrane sector (F0) of the ATP synthase complex are communicated to F1, thereby altering the binding characteristics of ATP to the beta subunits. By analogy, it is proposed that modifications (e.g., protonation/deprotonation) of the DCCD-binding protein effected by protonic energy alter the conformation of F1 and bring about the substrate/product binding changes that appear to be essential features of the mechanism and regulation of oxidative phosphorylation.
金褐霉素是一种荧光抗生素，它与线粒体F1 - ATP合酶的催化β亚基结合，抑制ATP的合成与水解。线粒体亚基颗粒（SMP）中的ATP、ADP和膜电位变化会改变与F1结合的金褐霉素的荧光。这些荧光变化被认为是对F1 - ATP合酶构象变化的响应。本文表明，当用寡霉素或N，N'-二环己基碳二亚胺（DCCD）预处理这些制剂时，与SMP或复合物V（纯化的ATP合酶复合物F0 - F1）结合的金褐霉素的ATP诱导荧光变化受到抑制。而在分离的F1 - ATP合酶中未观察到这种抑制作用。这些结果及其他结果表明，ATP合酶复合物膜部分（F0）中DCCD结合蛋白的修饰会传递给F1，从而改变ATP与β亚基的结合特性。由此类推，有人提出，由质子能量引起的DCCD结合蛋白的修饰（例如质子化/去质子化）会改变F1的构象，并导致底物/产物结合变化，而这似乎是氧化磷酸化机制和调节的基本特征。
