Faster interprotein electron transfer in a [myoglobin, b5] complex with a redesigned interface

Peng Xiong, Judith M. Nocek, Josh Vura-Weis, Jenny V. Lockard, Michael R. Wasielewski, Brian M. Hoffman

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Abstract

Direct measurements of electron transfer (ET) within a protein-protein complex with a redesigned interface formed by physiological partner proteins myoglobin (Mb) and cytochrome b5 (b5) reveal interprotein ET rates comparable to those observed within the photosynthetic reaction center. Brownian dynamics simulations show that Mb in which three surface acid residues are mutated to lysine binds b5 in an ensemble of configurations distributed around a reactive most-probable structure. Correspondingly, charge-separation ET from a photoexcited singlet zinc porphyrin incorporated within Mb to the heme of b5 and the follow-up charge-recombination exhibit distributed kinetics, with median rate constants, kf s = 2.1 × 109 second-1 and k bs = 4.3 × 1010 second-1, respectively. The latter approaches that for the initial step in photosynthetic charge separation, k = 3.3 × 1011 second-1.

Original languageEnglish
Pages (from-to)1075-1078
Number of pages4
JournalScience
Volume330
Issue number6007
DOIs
Publication statusPublished - Nov 19 2010

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Cite this

Xiong, P., Nocek, J. M., Vura-Weis, J., Lockard, J. V., Wasielewski, M. R., & Hoffman, B. M. (2010). Faster interprotein electron transfer in a [myoglobin, b5] complex with a redesigned interface. Science, 330(6007), 1075-1078. https://doi.org/10.1126/science.1197054