CaltechAUTHORS
Published September 1, 1997 | Version public
Journal Article Metadata-only

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

Creators

  • 1. ROR icon University of Minnesota
  • 2. ROR icon University of Wisconsin–Madison
  • 3. ROR icon Virginia Tech
  • 4. ROR icon California Institute of Technology

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

Identifiers

Eprint ID
54434
DOI
10.1016/S0040-4020(97)00710-2
Resolver ID
CaltechAUTHORS:20150205-140103112

Related works

Describes
10.1016/S0040-4020(97)00710-2 (DOI)

Funding

NSF
MCB-9513512
NSF
MCB-9317059
NSF
MCB-9630127
NSF
DMB 91-18689

Dates

Created
2015-02-08
Created from EPrint's datestamp field
Updated
2021-11-10
Created from EPrint's last_modified field