Active-site α-helix in papain and the stability of the ion pair RS− ··· ImH+. Ab initio molecular orbital study

Ab initio MO calculations, using both minimal (STO -3G) and extended (Roos–Siegbahn) basis sets are reported for the systems methanethiol–imidazole, methanethiol–imidazole–formaldehyde, and methanethiol–imidazole–formamide, which, together with a point-change representation of a long α-helix, form models for the active site of papain. It is shown that the large electric field exerted by the helix in the active-site region is responsible for the presence of the essential residues Cys 25 and His 159 in the form of an ion pair RS^? ··· ImH⁺, which is crucial for a recently proposed mechanism for the catalytic action of the enzyme. Also, an explanation is given for the anomalies in measured pK values for these residues. Detailed studies on the (sub)systems show that minimal basis sets lack the flexibility necessary for describing the type of proton transfer involved. We conclude that α-helices are essential parts of enzymes and that they play a significant role in the catalytic process.     

Polarized X-ray absorption study of Bi2Sr2CuO6 and Bi2Sr2CaCu2O8

Polarization dependent X-ray absorption measurements on single crystal Bi₂Sr₂CuO₆ (T _c =9 K) and Bi₂Sr₂CaCu₂O₈ (T _c =80 K) with one and two CuO₂ layers, respectively, show no energy shift of the Cu 2p main peak, and no relation between the amount of 3d(m=0, ±1) character and the critical temperatureT _c . At grazing incidence a structure in Bi₂Sr₂CaCu₂O₈ is found at 937 eV, which can be ascribed to a composite state of Cu 3d(z ²), Cu 4s ando–2p(z).