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Electron tunneling in proteins: role of the intervening medium (1997)

Winkler, J. R. ; Gray, H. B.

Springer

JBIC 2 (1997), S. 399-404

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ISSN: 1432-1327

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology

Notes: Abstract Analysis of electron-transfer (ET) kinetics data obtained from experiments on Ru-modified proteins (cytochrome c, azurin, myoglobin) reveals that distant donor-acceptor electronic couplings depend upon the secondary structure of the intervening polypeptide matrix. Rates of Fe2+→Ru3+ ET reactions in cytochrome c decay exponentially with tunneling-pathway length (decay constant 0.73 Å–1); these rates also decay exponentially with Ru-Fe distance (decay constant 1.1 Å–1). In azurin, a β-sheet protein, Cu+→Ru3+ rates exhibit an exponential Cu-Ru distance dependence with a decay constant of 1.1 Å–1. Comparison of distant couplings in azurin and myoglobin suggests that hydrogen bonds are better mediators across β sheets than through α helices.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s007750050150

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