Mechanical coupling in the nitrogenase complex
Fig 6
Important residues for mechanical coupling between (A) Fe1 and α1β1, (B) Fe1 and Fe2 and (C) P-loops in Fe1 and P-loops in Fe2 as identified by cost-weighted betweenness centrality, χ. For clarity, only residues with χ > 40% of maximum value are shown as hot pink space-filling structures, whose size is proportional to the magnitude of the corresponding χ value. The ribbon presentation of the ATP-bound nitrogenase complex is colored as follows: Fe1, red; Fe2, yellow; α1β1 unit of MoFe, blue; α2β2 unit of MoFe, green. ATP, [4Fe-4S] clusters, P-clusters and FeMo-co are shown in spheres. Residues among top 10% of χ or residues in/near the sites of interest are labeled.