Related Experiment Video
Updated: Jul 18, 2026

Synthetic Methodology for Asymmetric Ferrocene Derived Bio-conjugate Systems via Solid Phase Resin-based Methodology
Published on: March 12, 2015
Nitrogen binding to the FeMo-cofactor of nitrogenase
Johannes Schimpl1, Helena M Petrilli, Peter E Blöchl
1Institute for Theoretical Physics, Clausthal University of Technology, D-38678 Clausthal-Zellerfeld, Germany.
Abstract:
Density functional calculations are presented to unravel the first steps of nitrogen fixation of nitrogenase. The individual steps leading from the resting state to nitrogen binding at the FeMo-cofactor with a central nitrogen ligand are characterized. The calculations indicate that the Fe-Mo cage opens as dinitrogen binds to the cluster. In the resting state, the central cage is overall neutral. Electrons and protons are transferred in an alternating manner. Upon dinitrogen binding, one protonated sulfur bridge is broken. An axial and a bridged binding mode of dinitrogen have been identified. Adsorption at the Mo site has been investigated but appears to be less favorable than binding at Fe sites.
Related Concept Videos
Induced-fit Model
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Cofactors and Coenzymes
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Cofactors and Coenzymes
Introduction to Mechanisms of Enzyme Catalysis
Cofactors and Coenzymes
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...

