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

Magnuson, Jon K. and Paustian, Timothy D. and Shah, Vinod K. and Dean, Dennis R. and Roberts, Gary P. and Rees, Douglas C. and Howard, James B. (1997) Nitrogenase Iron-Molybdenum Cofactor Binding Site: Protein Conformational Changes Associated with Cofactor Binding. Tetrahedron, 53 (35). pp. 11971-11984. ISSN 0040-4020. doi:10.1016/S0040-4020(97)00710-2.

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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.

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Rees, Douglas C.0000-0003-4073-1185
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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.
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NSFDMB 91-18689
Issue or Number:35
Record Number:CaltechAUTHORS:20150205-140103112
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Official Citation:Jon K. Magnuson, Timothy D. Paustian, Vinod K. Shah, Dennis R. Dean, Gary P. Roberts, Douglas C. Rees, James B. Howard, Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding, Tetrahedron, Volume 53, Issue 35, 1 September 1997, Pages 11971-11984, ISSN 0040-4020, (
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ID Code:54434
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Deposited On:08 Feb 2015 03:26
Last Modified:10 Nov 2021 20:33

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