The scanning probe microscopy of metalloproteins and metalloenzymes.
In recent years, the concept of microscopy and the ability to study processes at a truly molecular level have been revolutionised by the development of a family of instruments based on acquiring data through the scanning of a proximal probe across a surface. Scanning Probe Microscopes (SPMs) enable surface-confined structures to be resolved at ångstrom-resolution, in real time, and under a variety of controllable conditions. Despite initial difficulties, much progress has been in the application of this technology to the high-resolution analysis of biological systems; these have varied from complex cellular systems to molecular biopolymers. Studying the interactions of protein with surfaces has been intrinsic to the development of our understanding of blood coagulation, fibrinolysis, thrombus formation and the synthesis of biocompatible materials. The specific interactions of metalloproteins and enzymes with electrode surfaces remains central to the understanding of the bioelectrochemical processes and to the development of biosensing devices. Though ellipsometry, Raman, microcalorimetry, surface plasmon resonance, and other spectroscopic methods, can provide much information on these interfaces, the acquired data are averaged over a large number of molecular species with a low spatial resolution. Proximal probe methods have much to offer in this regard and have revolutionized our ability to monitor such interactions.
Inorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK OX1 3QR.
Jason J
JJ
Davis
H Allen O
HA
Hill
D000818:Animals; D004798:Enzymes / Q000737:chemistry*; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008667:Metalloproteins / Q000737:chemistry*; D020527:Microscopy, Scanning Probe / Q000295:instrumentation / Q000639:trends*; D011487:Protein Conformation
D004798:Enzymes; D008667:Metalloproteins