作者: M. Klingenberg , M. Appel
DOI: 10.1016/0014-5793(80)81029-5
关键词: Biochemistry 、 Cytosol 、 Amino acid 、 Chemistry 、 ATP–ADP translocase 、 Protein subunit 、 Membrane 、 Biophysics 、 Substrate (chemistry) 、 Binding site 、 Chemiosmosis
摘要: The unique availability of two groups highly specific inhibitors the ADP, ATP carrier has made it possible to gain a advanced insight into mechanism on molecular level. In particular, binding studies with [l] and inhibitors, atractylate (ATR), carboxyatractylate (CAT) [2-41 bongkrekate (BKA) [3,5-71 led us in elaborate since 1969 discovery reorientation [6-81 its version which we called 1976 ‘gated pore’ [9-l 11. As consequence been postulated exist essentially major states, alternating translocation process, ‘c-state’ where single site is facing cytosolic side membrane can bind CAT, ‘m-state’ matrix BKA. both states high specificity for ADP ATP. Different from our models, separate ATR was proposed be located control subunit linked [12,13]. Lauquin Vignais maintained that also BKA bound sites forms ternary BKA-ADP protein complex [14,15]. Our model explicitly excludes this complex, first 1970 [5], but then ruled out by an abundance evidence 1972 [6,7]. Then, fixed gated pore dimeric substrate at same adopted [16,17]. localization outer