These data resolve a distance heterogeneity in the short Mn–Mn distances of the S1 and S2 state and thereby provide firm evidence for three Mn–Mn NVP-HSP990 distances between ~2.7 and ~2.8 Å (Yano et al. 2005a; Pushkar et al. 2007). This result gives clear criteria for selecting and refining possible structures from the repertoire of proposed models based on spectroscopic and diffraction data. Polarized XAS Polarized XAS studies on oriented membranes Membrane proteins like PS II can be oriented on a substrate such that the lipid membrane planes are roughly parallel to the substrate surface. This imparts a one-dimensional order to these samples, while the z-axis for each

membrane (collinear with the membrane normal) is roughly parallel to the substrate normal, the x and y axes remain disordered. Exploiting the plane-polarized nature of synchrotron radiation, spectra can be collected at different angles between the substrate normal and the X-ray E vector. The dichroism, which is the dependence of the intensity of the absorber–backscatterer pairs present in the oriented samples as a function of the polarization of the X-rays, is reflected in, and can be extracted from,

the resulting X-ray absorption selleck kinase inhibitor spectra (George et al. 1989, 1993). The EXAFS of the oriented PS II samples exhibits distinct dichroism, from which we have deduced the learn more relative orientations of several interatomic vector directions BCKDHB relative to the membrane normal and derived a topological representation of the metal sites in the OEC (Mukerji et al. 1994; Dau et al. 1995; Cinco et al. 2004; Pushkar et al. 2007). To a first order approximation, the angle dependence of the EXAFS is proportional to cos2(θ ER), with θ ER being the angle between the X-ray electric field vector (E) and the absorber–backscatter vector (R) (Fig. 5a). In turn, θ ER is composed of the detection angle θ and the angle ϕ between R and M, the membrane normal. Due to the rotational symmetry of the layered membranes, the angle ϕ defines a cone around the membrane normal M. When membranes are layered on a flat

substrate, the preferential orientation of M is parallel to the underling substrate normal (S). For those imperfectly stacked sheets, the probability (P α) of finding an angle α between M and S is the product of sinα and the order function P ord(α), which is maximal at α = 0°. P ord(α) is approximated by a Gaussian distribution whose half-width is the mosaic spread (Ω) or the disorder angle. Here, the mosaic spread is assumed to account for the disorder between the membrane normal and substrate normal, while the spread of R relative to M is negligible. For an ensemble of A–B vectors (R), the magnitude of the EXAFS is related to the P α-weighted integration over all possible orientations of M (α- and β-integration) and along the cone of the possible directions of R (γ-integration). Fig.