Electron bifurcation is the recently recognized third mechanism of biological energy conservation. It simultaneously couples exergonic and endergonic oxidation-reduction reactions to circumvent thermodynamic barriers and minimize free energy loss. Little is known about the details of how electron bifurcating enzymes function, but specifics are beginning to emerge for several bifurcating enzymes. To date, those characterized contain a collection of redox cofactors including flavins and iron-sulfur clusters. Here we discuss the current understanding of bifurcating enzymes and the mechanistic features required to reversibly partition multiple electrons from a single redox site into exergonic and endergonic electron transfer paths.
|Number of pages||7|
|Journal||Current Opinion in Chemical Biology|
|State||Published - Apr 1 2016|
Bibliographical noteFunding Information:
This work is supported as part of the Biological and Electron Transfer and Catalysis (BETCy) EFRC, an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science ( DE-SC0012518 ). P.W.K. was supported by the U.S. Department of Energy under contract no. DE-AC36-08-GO28308 with the National Renewable Energy Laboratory. We thank the entire BETCy team for helpful discussions.
ASJC Scopus subject areas
- Analytical Chemistry