Optimal photoelectron circular dichroism of a model chiral system.

We optimize the internuclear geometry and electronic structure of a model chiral system to achieve a maximal photoelectron circular dichroism (PECD) in its one-photon ionization by circularly polarized light. The electronic structure calculations are performed by the single center method, while the optimization is done using quantum alchemy employing a Taylor series expansion. Thereby, the effect of bond lengths and uncompensated charge distributions on the chiral response of the model is investigated theoretically in some detail. It is demonstrated that manipulating a chiral asymmetry of the ionic potential may enhance the dichroic parameter (i.e., the PECD) of the randomly oriented model system well beyond ß1 = 25%. Furthermore, we demonstrate that quantum alchemy is applicable to PECD despite the unusually strong coupling of spatial and electronic degrees of freedom and discuss the relative impact of the individual degrees of freedom in this model system. We define the necessary conditions for the computational design of PECD for real (non-model) chiral molecules using our approach.

Cysteine Linkages Accelerate Electron Flow through Tetra-Heme Protein STC.

Multi-heme proteins have attracted much attention recently due to their prominent role in mediating extracellular electron transport (ET), but one of their key fundamental properties, the rate constants for ET between the constituent heme groups, have so far evaded experimental determination. Here we report the set of heme-heme theoretical ET rate constants that define electron flow in the tetra-heme protein STC by combining a novel projector-operator diabatization approach for electronic coupling calculation with molecular dynamics simulation of ET free energies. On the basis of our calculations, we find that the protein limited electron flux through STC in the thermodynamic downhill direction (heme 1→4) is ∼3 × 106 s-1. We find that cysteine linkages inserting in the space between the two terminal heme pairs 1-2 and 3-4 significantly enhance the overall electron flow, by a factor of about 37, due to weak mixing of the sulfur 3p orbital with the Fe-heme d orbitals. While the packing density model, and to a higher degree, the pathway model of biological ET partly capture the predicted rate enhancements, our study highlights the importance of the atomistic and chemical nature of the tunneling medium at short biological tunneling distances. Cysteine linkages are likely to enhance electron flow also in the larger deca-heme proteins MtrC and MtrF, where heme-heme motifs with sub-optimal edge-to-edge distances are used to shuttle electrons in multiple directions.

Conformational Space of a Polyphilic Molecule with a Fluorophilic Side Chain Integrated in a DPPC Bilayer.

We investigate the conformational space of a polyphilic molecule with hydrophilic, lipophilic and fluorophilic parts inserted as a transmembrane agent into a dipalmitoylphosphatidylcholine bilayer by means of all-atom molecular dynamics simulations. Special focus is put on the competing structural driving forces arising from the hydrophilic, lipophilic and fluorophilic side chains and the aromatic backbone of the polyphile. We observe a significant difference between the lipophilic and the fluorophilic side chains regarding their intramembrane distribution. While the lipophilic groups remain membrane-centered, the fluorophilic parts tend to orient toward the phosphate headgroups. This trend is important for understanding the influence of polyphile agents on the properties of phospholipid membranes. From a fundamental point of view, our computed distribution functions of the side chains are related to the interplay of sterical, enthalpic and entropic driving forces. Our findings illustrate the potential of rationally designed membrane additives which can be exploited to tune the properties of phospholipid membranes. © 2017 Wiley Periodicals, Inc.