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Figure 3
Comparison of the conformation of residues potentially involved in electron transfer at the interface between the tethered cyt c domain and the core domain of (A) wtRpNiR, (B) Ser321Met RpNiR and (C) NO-bound wtRpNiR. Potential electron transfer routes from Cys364 to Tyr323 are represented by red arrows, and from Cys367 to His143 by blue arrows. In the Ser321Met mutant, the side chain of Met321 replaces the water that connects the cyt c domain to the core domain. Ser321Met is shown in magenta and orange, and wild type is shown in grey and blue. The red spheres are water molecules and deep blue spheres are copper ions. The black dashed lines represent hydrogen bonds, yellow dashed lines through-bonds and red dashed lines the interactions involving copper sites.

IUCrJ
Volume 13| Part 4| July 2026|
ISSN: 2052-2525
https://doi.org/10.1107/S2052252526004549