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Published September 1, 1997 | public
Journal Article

Nitrogenase Iron-Molybdenum Cofactor Binding Site: Protein Conformational Changes Associated with Cofactor Binding

Abstract

Formation of active nitrogenase MoFe-protein requires the assembly and insertion of a unique molybdenum containing Fe:S cluster, the FeMoco. The protein acceptor is held in an open conformation by the binding of a small molecular weight protein, γ. Using selective alkylation of the protein cysteines, conformational changes associated with γ binding and cofactor insertion were evaluated and a model for the change presented. Reversible oxygen damage to the precursor is identified and evaluated in terms of the chemistry of dithionite used in the buffer as an oxygen scavenger.

Additional Information

© 1997 Elsevier Science Ltd. Received 10 April 1997; accepted 12 June 1997. This work was supported by NSF grants MCB-9513512 (JBH), MCB-9317059 (GR), MCB-9630127 (DD) and DMB 91-18689.

Additional details

Created:
August 19, 2023
Modified:
October 20, 2023