During the past year, we have extended our previous work [1] on the, Scanning Tunneling Microscopy (STM) of modified electrodes to the investigation of metalloproteins and metalloenzyme in aqueous solution. For example, we studied [2] the STM of metallothionein, a zinc-containing protein whose role is intimately involved in zinc-transfer in eukaryotes.
More recently, we have extended these studies to metalloenzymes, particularly [3] cytochrome P450, paying particular attention to the STM of mutant proteins which we believe would aid the acquisition of STM at higher resolution. We are currently investigating the formation of complexes between cytochrome P450 and its natural partner, putidaredoxin, in the attempt to acquire information on electron transfer with this complex.
In our desire to extend the use of the method to more intact biological materials, we are currently studying [4] the Atomic Force Microscopy of cardiac muscle cells and it is encouraging the amount of information that can readily be obtained.
References1. J.J Davis, H.A.O. Hill, R. Yamada, H. Naoharsa and K. Uosaki, Scanning Tunneling Microscopy Study of the self assembly of 2-mercaptopyrimidine and 4,6-dimethyl-2-Mercaptopyrimidine on Au(111), J. Chem. Soc. Farad. 1998, 94, 1315-1319.2. Davis, H.A.O. Hill, A. Kurz, C. Jacob, W. Maret, B.L. Vallee, Phys. Chem. Comm. 1998, 2 3. Davis H.A.O. Hill, P. Kyritsis, K. Lo, L-L. Wong to be published4. Davis, H.A.O. Hill, T. Powell, to be published