Control of electron transfer in nitrogenase
- Seefeldt, Lance C. [ Department of Chemistry and Biochemistry, Utah State University, 0300 Old Main Hill, Logan, UT 84322, USA ]
- Peters, John W. [ Institute of Biological Chemistry, Washington State University, 287 Clark Hall, Pullman, WA 99164, USA ]
- Beratan, David N. [ Departments of Chemistry, Physics, and Biochemistry, Duke University, Durham, NC 27708 and 27710, USA ]
- Bothner, Brian [ Montana State University: Chemistry & Biochemistry ]
- Minteer, Shelley D. [ Departments of Chemistry and Materials Science & Engineering, University of Utah, 315 S 1400 E, Salt Lake City, UT 84112, USA ]
- Raugei, Simone [ Physical and Computational Sciences, Pacific Northwestern National Laboratory, 602 Battelle Blvd, Richland, WA 99352, USA ]
- Hoffman, Brian M. [ Department of Chemistry, Northwestern University, Evanston, IL 60208, USA ]
The bacterial enzyme nitrogenase achieves the reduction of dinitrogen (N2) to ammonia (NH3) utilizing electrons, protons, and energy from the hydrolysis of ATP. Building on earlier foundational knowledge, recent studies provide molecular-level details on how the energy of ATP hydrolysis is utilized, the sequencing of multiple electron transfer events, and the nature of energy transduction across this large protein complex. Here, we review the state of knowledge about energy transduction in nitrogenase.