Alkyne substrate interaction within the nitrogenase MoFe protein
- 29 May 2007
- journal article
- Published by Elsevier in Journal of Inorganic Biochemistry
- Vol. 101 (11-12) , 1642-1648
- https://doi.org/10.1016/j.jinorgbio.2007.05.007
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Intermediates Trapped during Nitrogenase Reduction of N⋮N, CH3−NNH, and H2N−NH2Journal of the American Chemical Society, 2005
- Substrate Interactions with the Nitrogenase Active SiteAccounts of Chemical Research, 2005
- The Mechanism of Nitrogenase. Computed Details of the Site and Geometry of Binding of Alkyne and Alkene Substrates and IntermediatesJournal of the American Chemical Society, 2004
- Localization of a Catalytic Intermediate Bound to the FeMo-cofactor of NitrogenaseJournal of Biological Chemistry, 2004
- An Organometallic Intermediate during Alkyne Reduction by NitrogenaseJournal of the American Chemical Society, 2004
- Substrate Interactions with Nitrogenase: Fe versus MoBiochemistry, 2004
- Localization of a Substrate Binding Site on the FeMo-Cofactor in Nitrogenase: Trapping Propargyl Alcohol with an α-70-Substituted MoFe ProteinBiochemistry, 2003
- Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-CofactorScience, 2002
- Catalytic and Biophysical Properties of a Nitrogenase Apo-MoFe Protein Produced by a nifB-Deletion Mutant of Azotobacter vinelandiiBiochemistry, 1998
- Crystallographic Structure of the Nitrogenase Iron Protein from Azotobacter vinelandiiScience, 1992