Literature summary for 1.7.5.1 extracted from

Seif Eddine, M.; Biaso, F.; Rendon, J.; Pilet, E.; Guigliarelli, B.; Magalon, A.; Grimaldi, S.
1,2H hyperfine spectroscopy and DFT modeling unveil the demethylmenasemiquinone binding mode to E. coli nitrate reductase A (NarGHI) (2020), Biochim. Biophys. Acta Bioenerg., 1861, 148203 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
NarGHI	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	demethylmenasemiquinone and menasemiquinone bind in a similar and strongly asymmetric manner through a short H-bond, caused by slightly inequivalent contributions from two beta-methylene protons of the isoprenoid side chain. Their large isotropic hyperfine coupling constants are consistent with both a specific highly asymmetric binding mode of (demethyl)menasemiquinone and a near in-plane orientation of its isoprenyl chain at Cbeta relative to the aromatic ring, which differs by about 90° to that predicted for free or NarGHI-bound menaquinol	Escherichia coli

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Release 2023.1 (January 2023)