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. 2023 Dec 7;31(1):150–158. doi: 10.1038/s41594-023-01124-2

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a, Left: Depiction of the AnfDGKH₂ subcomplex. Right: Electrostatic potentials of the AnfH₂ (top) and AnfDGK (bottom) interaction surfaces. Negative charges are in red, neutral in white and positive in blue. Arrows indicate interaction interfaces with complementary charges. AnfG is outlined in black. b, Left: Depiction of the NifDKH₂ subcomplex (modified from PDB 7UTA). Right: Electrostatic surface potentials as shown in a. c, Close-up view of the AnfG–AnfH interaction interface as highlighted in a. Hydrogen bonds between amino acid residues are indicated by white dashes. Shown in faint blue is Asp69^NifH that replaces Arg69^AnfH in the Mo nitrogenase complex (PDB 7UTA), exemplifying the reverse interaction characteristics of the two reductase components. d, A 90° rotation from the view in c toward the FeFeco showing two CAVER predicted channels to the active site (Ch-1 and Ch-2; tubes in different shades of gray) and an N₂ channel calculated using molecular dynamics proposed by ref. ⁴⁸ (purple residues). Light-blue dashes highlight interactions of AnfG residues Ser25^AnfG and Glu109^AnfG with residues of the channel calculated using molecular dynamics. White dashes depict the same interactions highlighted in c. e, Left: Per-atom B factors within the Fe nitrogenase complex. Right: Highlight of B factors in the αIII domain and AnfG in putty representation. f, Model of apo-Anf(DGK)₂ fitted into the 2.49-Å cryo-EM map of the CHAPSO detergent-treated Anf(DGK)₂ sample (PDB 8PBB; EMD-17583). As highlighted by the arrows, electron density for AnfG and parts of AnfD is missing, including the αIII domain and the FeFeco.