December 22, 2010 :: Professor Michael R. Wasielewski and researchers at the
Argonne-Northwestern Solar Research (ANSER) Center, a DOE Energy Frontier Research Center, in collaboration with Professor Brian M. Hoffman of Northwestern University have designed a protein-protein complex with the fastest recorded interprotein electron transfer rate constant (4.3 x10
10 s
-1). Brownian dynamics simulations predicted that substituting three surface acid residues in myoglobin (Mb) with lysine binds cytochrome b5 (b5) strongly in an ensemble of bound configurations. Femtosecond transient absorption measurements of the redesigned protein-protein interface led to a range of ultrafast electron transfer rates (10
9 to 10
10 s
-1) that approach those occurring within natural photosynthetic reaction centers (photosystem I and photosystem II, 10
11 to 10
12 s
-1). In contrast, most biological interprotein electron transfer processes are typically many orders of magnitude slower (10
6 s
-1). This work demonstrates that efficient photodriven charge transfer can take place between complex, self-assembled structures and holds promise for achieving such behavior in systems designed for artificial photosynthesis. These results were reported in
Science and highlighted in
Chemical and Engineering News.
Reference: Xiong, P.; Nocek, J. M.; Vura-Weis, J.; Lockard, J. V.; Wasielewski, M. R.; and Hoffman, B. M., Faster Interprotein Electron Transfer in a [Myoglobin, b5] Complex with a Redesigned Interface,
Science,
330, 1075-1078 (2010) [
DOI:10.1126/science.1197054]; Jyllian N. Kemsely, Speedier Electron Transfer,
Chemical and Engineering News,
88, 27 (Nov. 22, 2010).