Erratum: Publisher's Note: "Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer" [Struct. Dyn. 1, 024701 (2014)].

[This corrects the article DOI: 10.1063/1.4869472.].

Enhanced hydrogenation activity and diastereomeric interactions of methyl pyruvate co-adsorbed with R-1-(1-naphthyl)ethylamine on Pd(111).

Unmodified racemic sites on heterogeneous chiral catalysts reduce their overall enantioselectivity, but this effect is mitigated in the Orito reaction (methyl pyruvate (MP) hydrogenation to methyl lactate) by an increased hydrogenation reactivity. Here, this effect is explored on a R-1-(1-naphthyl)ethylamine (NEA)-modified Pd(111) model catalyst where temperature-programmed desorption experiments reveal that NEA accelerates the rates of both MP hydrogenation and H/D exchange. NEA+MP docking complexes are imaged using scanning tunnelling microscopy supplemented by density functional theory calculations to allow the most stable docking complexes to be identified. The results show that diastereomeric interactions between NEA and MP occur predominantly by binding of the C=C of the enol tautomer of MP to the surface, while simultaneously optimizing C=O····H2N hydrogen-bonding interactions. The combination of chiral-NEA driven diastereomeric docking with a tautomeric preference enhances the hydrogenation activity since C=C bonds hydrogenate more easily than C=O bonds thus providing a rationale for the catalytic observations.

Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer.

With recent technological advances at synchrotrons [Graber et al., J. Synchrotron Radiat. 18, 658-670 (2011)], it is feasible to rapidly collect time-resolved crystallographic data at multiple temperature settings [Schmidt et al., Acta Crystallogr. D 69, 2534-2542 (2013)], from which barriers of activation can be extracted. With the advent of fourth generation X-ray sources, new opportunities emerge to investigate structure and dynamics of biological macromolecules in real time [M. Schmidt, Adv. Condens. Matter Phys. 2013, 1-10] in crystals and potentially from single molecules in random orientation in solution [Poon et al., Adv. Condens. Matter Phys. 2013, 750371]. Kinetic data from time-resolved experiments on short time-scales must be interpreted in terms of chemical kinetics [Steinfeld et al., Chemical Kinetics and Dynamics, 2nd ed. (Prentience Hall, 1985)] and tied to existing time-resolved experiments on longer time-scales [Schmidt et al., Acta Crystallogr. D 69, 2534-2542 (2013); Jung et al., Nat. Chem. 5, 212-220 (2013)]. With this article, we will review and outline steps that are required to routinely determine the energetics of reactions in biomolecules in crystal and solution with newest X-ray sources. In eight sections, we aim to describe concepts and experimental details that may help to inspire new approaches to collect and interpret these data.

Three-dimensional single-particle imaging using angular correlations from X-ray laser data.

Femtosecond X-ray pulses from X-ray free-electron laser sources make it feasible to conduct room-temperature solution scattering experiments far below molecular rotational diffusion timescales. Owing to the ultra-short duration of each snapshot in these fluctuation scattering experiments, the particles are effectively frozen in space during the X-ray exposure. In contrast to standard small-angle scattering experiments, the resulting scattering patterns are anisotropic. The intensity fluctuations observed in the diffraction images can be used to obtain structural information embedded in the average angular correlation of the Fourier transform of the scattering species, of which standard small-angle scattering data are a subset. The additional information contained in the data of these fluctuation scattering experiments can be used to determine the structure of macromolecules in solution without imposing symmetry or spatial restraints during model reconstruction, reducing ambiguities normally observed in solution scattering studies. In this communication, a method that utilizes fluctuation X-ray scattering data to determine low-resolution solution structures is presented. The method is validated with theoretical data calculated from several representative molecules and applied to the reconstruction of nanoparticles from experimental data collected at the Linac Coherent Light Source.