SCOPE AND AIM One of the main goals of modern protein chemistry is the understanding of structure-function relationships in biological molecules, that is, how a molecule with a precise spatial conformation and specific properties plays a particular role in the gearing of the cellular machinery. This is what we now call "molecular recognition", the means by which molecules recognize other molecu...

EUROBIC is the European Bioinorganic Chemistry Conference and is organized by scientists from several European countries. This is the second edition of a biennial series on Metal Ions in Biological Systems. The conference is organized with the goal to overcome the scientific barriers among the European scientists and to develop and reinforce European scientific interactions. On the occasion of ...

In recent years, a number of high-valent iron intermediates have been identified as reactive species in iron-containing metalloproteins. Inspired by the interest in these highly reactive species, chemists have synthesized Fe(IV) and Fe(V) model complexes with terminal oxo or nitrido groups, as well as a rare example of an Fe(VI)-nitrido species. In all these cases, X-ray absorption spectroscopy...

A spectrograph has been developed with sufficient efficiency to make high-resolution fluorescence experiments on metalloproteins possible. The resolution of this spectrometer can reach 0.45 eV at 7.1 keV emission energy. The focus images of this multiple curved-crystal array spectrometer are presented. The chemical sensitivity of Kbeta emission spectra can be used to identify chemical states, a...

Electron-transfer kinetics of the thermophilic protein Plastocyanin from Phormidium laminosum adsorbed on 1,ω-alkanedithiol self-assembled monolayers (SAMs) deposited on gold have been investigated. The standard electron-transfer rate constant has been determined as a function of electrode-protein distance and solution viscosity over a broad temperature range (0-90 °C). For either thin or thick...

The reduction potential (E°') is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes of metalloproteins to cover the majority of the 2-V range of physiological E°'s. An ultimate test of our understanding of E°' is to find out the minimal number of proteins and their variants that can cover this entire range and the structur...

The direct observation of binding and release of spectroscopically silent metal ions such as Zn(2+) and Ca(2+) by proteins has been challenging before the advent of native electrospray ionisation mass spectrometry. This report highlights the powerful capability of ESI-MS to provide insight into metalloprotein speciation that is independent of any spectroscopic property. Using the zinc-binding p...

Session I" Overview of the Chemistry and Biochemistry of Nitrogen Oxides Prof. L. Ignarro, UCLA: The Biology of Nitric Oxide Prof. J. Enemark, Arizona: Transition Metal Complexes of Nitrogen Oxides Prof. W. Koppenol, ETH Zurich: Fundamental Chemistry of Nitrogen Oxides Prof. S. Bohle, Wyoming: Synthesis and Characterization of Higher Nitrogen Oxides Prof. J. Lipscomb, Minnesota: Nitric Oxide as...

Featured Keynote Speaker Prof. Brian Gibney CUNY Graduate Center While DNA is the blueprint for the cell, it is the proteins that do the bulk of the work. About 30% of proteins require metal ions for proper function and their dysfunction leads to human disease. The Gibney Lab takes a constructive approach toward understanding metalloprotein structurefunction relationships. Using inorganic chemi...