The Home Page of Bo G. Malmström

Picture of Bo Picture of the CuA site

The research interests of Bo G. Malmström encompass three major problem areas:

  1. the structural and mechanistic basis for the function of terminal oxidases, particularly cytochrome c oxidase, as redox-linked proton pumps;
  2. protein folding in redox metalloproteins, particularly azurin; and
  3. the membrane penetration of modified PNA (peptide nucleic acid) molecules.
In the first area, recent work has been focussed on the primary electron acceptor in the oxidase, CuA, which has been expressed as a soluble domain. This has allowed for the first time the recording of the complete optical spectrum of this redox site, and the electronic structure and spectra are now being studied by semi-empirical and ab initio methods. The dynamic solution structure of the domain is being investigated by 3D NMR. The electron transfer to and from CuA will be measured in protein labelled with Ru.

The folding energy for oxidized and reduced azurin has been determined, and it was found that the oxidized protein is most stable. A thermodynamic consequence of this is that the unfolded, reduced protein has a higher reduction potential than the oxidized one, and the molecular basis of this finding is being studied.

PNA is a DNA analogue that has potential use as an antisense drug. A difficulty is, however, that it passes over phospholipid membranes very slowly, and modified PNAs with possibly enhanced penetration properties are now being investigated. This project is carried out in collaboration with the Department of Physical Chemistry, Chalmers University of Technology.

Recent publications 1993-

ÖH 1997-06-16