The photoreceptor protein cryptochrome is thought to host, upon light absorption, a radical pair that is sensitive to very weak magnetic fields, endowing migratory birds with a magnetic compass sense. The molecular mechanism that leads to formation of a stabilized, magnetic field sensitive radical pair has despite various theoretical and experimental efforts not been unambiguously identified yet. We challenge this unambiguity through a unique quantum mechanical molecular dynamics approach where we perform electron transfer dynamics simulations taking into account the motion of the protein upon the electron transfer. This approach allows us to follow the time evolution of the electron transfer in an unbiased fashion and to reveal the molecular driving force that ensures fast electron transfer in cryptochrome guaranteeing formation of a persistent radical pair suitable for magnetoreception. We argue that this unraveled molecular mechanism is a general principle inherent to all proteins of the cryptochrome/photolyase family and that cryptochromes are, therefore, tailored to potentially function as efficient chemical magnetoreceptors.

Future prospects of the organic light emitting diode (OLED) technology rely on the development of new organic semiconductors with optical and electronic properties outperforming those of presently available materials. Computational materials design is becoming a widely used tool to complement and accelerate experimental efforts. Computational tools were also shown to contribute to the understanding of experimentally observed phenomena. Impurities and charge traps are omnipresent in most currently available organic semiconductors and limit the charge transport and thus the efficiency of the devices. The microscopic cause as well as the chemical nature of these traps is presently not well understood. Using a multiscale model we characterize the influence of impurities on the density of states and charge transport in small-molecule amorphous organic semiconductors. We use the model to quantitatively describe the influence of water molecules and water-oxygen complexes on the electron and hole mobility by influencing the shape of the density of states and at the same time acting as explicit charge traps within the energy gap. Our results show that deep trap states introduced by molecular oxygen mainly determine the electron mobility in widely used materials such as α-NPD. TOC

We study fast hole transfer events in E. coli DNA photolyase, a key step in the photoactivation process, using a multiscale computational method that combines nonadiabatic propagation schemes and linear-scaling quantum chemical methods with molecular mechanics force fields. This scheme allows us to follow the time-dependent evolution of the electron hole in an unbiased fashion; that is, no assumptions about hole wave function localization, time scale separation, or adiabaticity of the process have to be made beforehand. DNA photolyase facilitates an efficient long-range charge transport between its flavin adenine dinucleotide (FAD) cofactor and the protein surface via a chain of evolutionary conserved Trp residues on the sub-nanosecond time scale despite the existence of multiple potential trap states. By including a large number of aromatic residues along the charge transfer pathway into the quantum description, we are able to identify the main pathway among alternative possible routes. The simulations show that charge transfer, which is extremely fast in this protein, occurs on the same time scale as the protein response to the electrostatic changes; that is, time-scale separation as often presupposed in charge transfer studies seems to be inappropriate for this system. Therefore, coupled equations of motion, which propagate electrons and nuclei simultaneously, appear to be necessary. The applied computational model is shown to capture the essentials of the reaction kinetics and thermodynamics while allowing direct simulations of charge transfer events on their natural time scale.

Cryptochrome proteins are activated by the absorption of blue light, leading to the formation of radical pairs through electron transfer in the active site. Recent experimental studies have shown that once some of the amino acid residues in the active site of Xenopus laevis cryptochrome DASH are mutated, radical-pair formation is still observed. In this study, we computationally investigate electron-transfer pathways in the X. laevis cryptochrome DASH by extensively equilibrating a previously established homology model using molecular dynamics simulations and then mutating key amino acids involved in the electron transfer. The electron-transfer pathways are then probed by using tight-binding density-functional theory. We report the alternative electron-transfer pathways resolved at the molecular level and, through comparison of amino acid sequences for cryptochromes from different species, we demonstrate that one of these alternative electron-transfer pathways could be general for all cryptochrome DASH proteins.

Excitation energy and charge transfer are fundamental processes in biological systems. Because of their quantum nature, the effect of dephasing on these processes is of interest especially when trying to understand their efficiency. Moreover, recent experiments have shown quantum coherences in such systems. As a first step toward a better understanding, we studied the relationship between dephasing time and energy gap fluctuations of the individual molecular subunits. A larger set of molecular simulations has been investigated to shed light on this dependence. This set includes bacterio-chlorophylls in Fenna-Matthews-Olson complexes, the PE545 aggregate, the LH2 complexes, DNA, photolyase, and cryptochromes. For the individual molecular subunits of these aggregates it has been confirmed quantitatively that an inverse proportionality exists between dephasing time and average gap energy fluctuation. However, for entire complexes including the respective intermolecular couplings, such a relation still needs to be verified.