Dr. M. Nonella
Marco Nonella studied chemistry at the University of Zürich, and carried out his doctoral thesis under Prof. J. Robert Huber in the Laboratory of Physical Chemistry of the University of Zürich (1986). Before he became Assistant Professor at the University of Zurich (1992), he worked as a postdoctoral in the Theoretical Biophysics Group of Prof. Klaus Schulten at the Beckman Institut at the University of Illinois at Urbana-Champaign (1988-1991) and in the Group of Prof. Dieter Oesterhelt at the Max-Planck-Institut of Biochemistry at Martinsried (1991-1992). From 1992 to 1998 he was Assistent Professor at the University of Zürich, first in the Institute of Physical Chemistry and later in the Institute of Biochemistry. In 1998 he accepted a position at the LMU in Munich sponsored by the Volkswagenstiftung.
Quantum chemical methods of different levels of approximation as well as classical molecular dynamics and electrostatics techniques are applied for investigating properties of important protein cofactors and mechanisms of biophysical processes. So far such investigations have been focussed on photosynthetic proteins like the photosynthetic reaction centers of Rhodopseudomonas viridis and Rhodobacter sphaeroides of the photosynthetic proton pump Bacteriorhodopsin.
In photosynthetic reaction centers we have in close collaboration with Jacques Breton and his group studied the structure and vibrational spectrum of quinones with modern density functional methods. Applying such methods, the vibrational frequencies of the C=C and C=O modes of quinones and their isotope shifts can be predicted very accurate and allows already a profound discussion of experimental data. Furthermore, the modeling of quinone protein interactions by investigating simple complexes of a quinone with hydrogen bond donors or charged molecules provides a detailed understanding of effects found in proteins.
In Bacteriorhodopsin we have focussed our studies of the very fast primary reaction of the photocycle and on electrostatic interactions of the chromophore with the protein environment. The primary reaction takes place on the potential energy surface of the first excited state. To allow a better understanding of this process we have calculated potential energy surfaces for various model molecules of protonated Schiff bases. In classical molecular dynamics simulations and in electrostatic calculations the accurate determination of chromophore protein interactions is important. We have therefore investigated the charge distribution of a protonated Schiff base with various quantum chemical methods and we have studied how different charge distributions affect intermolecular forces and calculated titration curves.
In the near future we will apply QM/MM hybrid techniques in our investigations on protein cofactor interactions and for the simulation of enzymatic reactions.
Last update: 24-May-99 / MN