机构:
UNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USAUNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA
MOSER, CC
[1
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KESKE, JM
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机构:
UNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USAUNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA
KESKE, JM
[1
]
WARNCKE, K
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机构:
UNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USAUNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA
WARNCKE, K
[1
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FARID, RS
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机构:
UNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USAUNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA
FARID, RS
[1
]
DUTTON, PL
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UNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USAUNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA
DUTTON, PL
[1
]
机构:
[1] UNIV PENN, DEPT BIOCHEM & BIOPHYS, JOHNSON RES FDN, PHILADELPHIA, PA 19104 USA
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 angstrom 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.