|
|
Article: Researchers at Utah State University have published new data on biological inorganic chemistry.
- Article from:
- Chemicals & Chemistry
- Article date:
- November 13, 2009
CopyrightCOPYRIGHT 2009 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan. All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)
|
"Nitrogenase catalyzes the six electron/six proton reduction of N-2 to two ammonia molecules at a complex organometallocluster called ''FeMo cofactor.'' This cofactor is buried within the alpha-subunit of the MoFe protein, with no obvious access for substrates. Examination of high-resolution X-ray crystal structures of MoFe proteins from several organisms has revealed the existence of a water-filled channel that extends from the solvent-exposed surface to a specific face of FeMo cofactor," researchers in the United States report.
"This channel could provide a pathway for substrate and product access to the active site. In the present work, we examine this ...