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Electron flow through metalloproteins

Gray, Harry (2016) Electron flow through metalloproteins. In: 251st American Chemical Society National Meeting & Exposition, March 13-17, 2016, San Diego, CA.

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Understanding the underlying physics and chem. of biol. electron transfer processes is the goal of much of the work in my lab. Employing laser flash-quench triggering methods, my coworkers and I have shown that long-range (1.5 to 2.5 nm) electron tunneling reactions in Ru-modified cytochromes and blue copper proteins occur on microsecond to nanosecond timescales. Redox equiv. can be transferred even longer distances by multistep tunneling (called hopping) through intervening tyrosines and tryptophans: notably, in our work on cytochrome P 450 and azurin, we have found that long-range hole hopping through intervening tryptophans can be orders of magnitude faster than single-step tunneling. Could hole hopping through Tyr/Trp chains protect redox enzymes from oxidative damage. Jay Winkler and I think so: by examg. the structures of P450s and many other oxygenases, we have identified conserved Tyr/Trp chains that could transfer holes rapidly from uncoupled high-potential intermediates to reductants in contact with protein surface sites.

Item Type:Conference or Workshop Item (Paper)
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Gray, Harry0000-0002-7937-7876
Additional Information:© 2016 American Chemical Society.
Record Number:CaltechAUTHORS:20160404-132052605
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:65897
Deposited By: Tony Diaz
Deposited On:05 Apr 2016 16:46
Last Modified:22 Nov 2019 09:58

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