Nature of biological electron transfer.
Powerful first-order analysis of intraprotein electron transfer is developed from electron-transfer measurements both in biological and in chemical systems. A variation of 20 A in the distance between donors and acceptors in protein changes the electron-transfer rate by 10(12)-fold. Protein presents a uniform electronic barrier to electron tunnelling and a uniform nuclear characteristic frequency, properties similar to an organic glass. Selection of distance, free energy and reorganization energy are sufficient to define rate and directional specificity of biological electron transfer, meeting physiological requirements in diverse systems.
Moser
C C
CC
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104.
Keske
J M
JM
Warncke
K
K
Farid
R S
RS
Dutton
P L
PL
D000818:Animals; D003574:Cytochrome c Group / Q000737:chemistry / Q000378:metabolism*; D004579:Electron Transport; D008433:Mathematics; D008954:Models, Biological; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism*; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D003574:Cytochrome c Group; D009211:Myoglobin; D045322:Photosynthetic Reaction Center Complex Proteins