Lardy H A, Schuster S M, Ebel R E
J Supramol Struct. 1975;3(3):214-21. doi: 10.1002/jss.400030303.
Evidence is presented that mitochondrial ATPase has two types of sites that bind adenine nucleotides. The catalytic site, C, binds the substrates ATP, GTP, or ITP and the inhibitor guanylyl imidodiphosphate (GMP-PNP). A second type of site, R, binds ATP, ADP, adenylyl imidodiphosphate (AMP-PNP), and the chromium complexes of ATP or ADP. All of these substances binding to the R site inhibit the hydrolysis of ATP in a competitive manner; their inhibition of hydrolysis of ITP and GTP is noncompetitive. GMP-PNP inhibits oxidative phosphorylation in submitochondrial particles but AMP-PNP does not. The localization on mitochondrial membranes of sites for the binding of various antibiotics that inhibit oxidative phosphorylation is discussed.
有证据表明，线粒体ATP酶有两类结合腺嘌呤核苷酸的位点。催化位点C结合底物ATP、GTP或ITP以及抑制剂鸟苷酰亚胺二磷酸（GMP-PNP）。第二类位点R结合ATP、ADP、腺苷酰亚胺二磷酸（AMP-PNP）以及ATP或ADP的铬配合物。所有这些与R位点结合的物质都以竞争性方式抑制ATP的水解；它们对ITP和GTP水解的抑制是非竞争性的。GMP-PNP抑制亚线粒体颗粒中的氧化磷酸化，但AMP-PNP则不然。本文还讨论了各种抑制氧化磷酸化的抗生素结合位点在线粒体内膜上的定位。
