Direct measurement of the hydrogen-bonding effect on the intrinsic redox potentials of [4Fe-4S] cubane complexes |
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Authors: | Yang Xin Niu Shuqiang Ichiye Toshiko Wang Lai-Sheng |
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Institution: | Department of Physics, Washington State University, 2710 University Drive, Richland, Washington 99352, USA. |
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Abstract: | To probe how H-bonding effects the redox potential changes in Fe-S proteins, we produced and studied a series of gaseous cubane-type analogue complexes, Fe(4)S(4)(SEt)(3)(SC(n)H(2n+1))](2-) and Fe(4)S(4)(SEt)(3)(SC(n)H(2n)OH)](2-) (n = 4, 6, 11; Et = C(2)H(5)). Intrinsic redox potentials for the Fe(4)S(4)](2+/3+) redox couple involved in these complexes were measured by photoelectron spectroscopy. The oxidation energies from Fe(4)S(4)(SEt)(3)(SC(n)H(2n)OH)](2-) to Fe(4)S(4)(SEt)(3)(SC(n)H(2n)OH)](-) were determined directly from the photoelectron spectra to be approximately 130 meV higher than those for the corresponding Fe(4)S(4)(SEt)(3)(SC(n)H(2n+1))](2-) systems, because of the OH...S hydrogen bond in the former. Preliminary Monte Carlo and density functional calculations showed that the H-bonding takes place between the -OH group and the S on the terminal ligand in Fe(4)S(4)(SEt)(3)(SC(6)H(12)OH)](2-). The current data provide a direct experimental measure of a net H-bonding effect on the redox potential of Fe(4)S(4)] clusters without the perturbation of other environmental effects. |
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