Fritz Haber Institute of the Max Planck Society

About: Fritz Haber Institute of the Max Planck Society is a facility organization based out in Berlin, Germany. It is known for research contribution in the topics: Catalysis & Adsorption. The organization has 3490 authors who have published 5017 publications receiving 183731 citations. The organization is also known as: Fritz Haber Institute of the Max Planck Society.

Electrochemical techniques for the study of photosensitization

Abstract: — Spectral photosensitization is discussed from an electrochemical point of view, as caused by electron transfer from or to excited molecules. General principles for a description of electron transfer processes at semiconductor or insulator electrodes are reviewed and applied to reactions which involve excited electronic states. The conditions for suitable experimental arrangements are characterized. Illustrations for the application of these techniques are given. The examples show spectral sensitization of photocurrents due to electron or hole injection into inorganic or organic solids.

Adsorption of Gases on Complex Solid Surfaces

Abstract: During the last thirty years the research field of surface science with its various disciplines has progressively played a more and more important role in the field of catalysis. The main focus of attention for a long time was research on metal surfaces, on which, in time, the whole spectrum of developed surface analytical methods was applied. This led to a better understanding of the mechanisms of catalytic reaction, such as the synthesis of ammonia and the oxidation of CO, especially through the work of Gerhard Ertl.[1, 2] In contrast to clean metal surfaces, surfaces of real catalysts are complex entities, the structures of which can have a strong influence on the processes occurring on the surface. Thus, it seems logical to employ the typical structural characteristics and the morphology of the catalytic surface as guidelines in the investigation of complex model systems. In this review the preparation, and structural and electronic characterization of such model systems will be dicussed. Clean surfaces of catalytically active oxides, as well as model systems for dispered transition metal/support catalysts will be characterized in terms of their morphology and electronic structure as well as their adsorption and reaction capabilities.

Dissociation of O2 at Al(111): the role of spin selection rules.

Abstract: A most basic and puzzling enigma in surface science is the description of the dissociative adsorption of O(2) at the (111) surface of Al. Already for the sticking curve alone, the disagreement between experiment and results of state-of-the-art first-principles calculations can hardly be more dramatic. In this Letter we show that this is caused by hitherto unaccounted spin selection rules, which give rise to a highly nonadiabatic behavior in the O(2)/Al(111) interaction. We also discuss problems caused by the insufficient accuracy of present-day exchange-correlation functionals.

The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry.

Abstract: Electron microscopy in combination with image processing is a powerful method for obtaining structural information on non-crystallized biological macromolecules at the 10-50 A resolution level. The processing of noisy microscopical images requires advanced data processing methodologies in which one must carefully avoid the introduction of any form of bias into the data set. Using a novel multivariate statistical approach to the analysis of symmetry, we studied the structure of the bacteriophage SPP1 portal protein oligomer. This portal structure, ubiquitous in icosahedral bacteriophages which package dsDNA, is located at the site of symmetry mismatch between a 5-fold vertex of the icosahedral shell and the 6-fold symmetric (helical) tail. From previous studies such 'head-to-tail connector' structures were generally accepted to be homododecamers assembled in a 12-fold symmetric ring around a central channel. Using a new analysis methodology we have found that the phage SPP1 portal structure exhibits 13-fold cyclical symmetry: a new point group organization for oligomeric proteins. A model for the DNA packaging mechanism by 13-fold symmetric portal protein assemblies is presented which attributes a coherent functional meaning to their unusual symmetry.