Single-molecule high-resolution structure and electron conduction of photosystem II from scanning tunneling microscopy and spectroscopy.
Scanning tunneling microscopy (STM) and spectroscopy (STS) were used to obtain the first direct high resolution ( approximately 0.3 nm) images of single isolated Photosystem II (PS II) molecules, and to determine the supramolecular organization of oxygen-evolving PS II core complexes and PS II membrane fragments including the identification, assignment, location and dimensions of the polypeptide units. Our results predict a unique structural model which we then compare with alternative models. We show that the combination of quasi-constant-height mode STM operation, STS and suitable choice of sample-substrate preparations can be used to enable investigation of the structure and function of single PS II particles under normal thermodynamic and hydration conditions without the requirement and complications of ordered PS II arrays or crystals. STS was also used to characterize single-molecule electron conduction and tunneling mechanisms in PS II including the semiconduction and photoconduction behavior of the reaction center and photoexcitation effects in the light-harvesting complex LHC II.
Lukins
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PB
School of Physics, A28, University of Sydney, Sydney, NSW 2006, Australia. lukins@physics.usyd.edu.au
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D004579:Electron Transport / Q000502:physiology*; D008565:Membrane Proteins / Q000648:ultrastructure; D016252:Microscopy, Scanning Tunneling; D010100:Oxygen / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000648:ultrastructure*; D045332:Photosystem II Protein Complex; D010940:Plant Proteins / Q000648:ultrastructure; D011487:Protein Conformation; D013057:Spectrum Analysis; D018724:Spinacia oleracea / Q000648:ultrastructure*
D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D010100:Oxygen