1.7.7.1	modeling of structure based on spinach nitrite reductase. Arginine and lysine residues are involved in electrostatically-stabilized binding to ferredoxin	
1.7.7.1	NMR-study of protein-protein interaction of ferredoxin and nitrite reductase shows three acidic regions of ferredoxin to be major sites for the interaction with the enzyme, indicating that the complex is stabilized through electrostatic interaction	
1.7.7.1	sitting drop vapour diffusion method	
1.7.7.1	the biological unit, NrfH2NrfA4, houses 28 c-type heme groups, 22 of them with low spin and 6 with pentacoordinated high spin configuration. The high spin hemes, which are the electron entry and exit points of the complex, carry a highly unusual coordination for c-type hemes, lysine and methionine as proximal ligands in NrfA and NrfH, respectively. The midpoint redox potential of the NrfH menaquinol-interacting methionine-coordinated heme is -270 mV	
1.7.7.1	the biological unit, NrfH2NrfA4, houses 28 c-type heme groups, 22 of them with low spin and 6 with pentacoordinated high spin configuration. The high spin hemes, which are the electron entry and exit points of the complex, carry a highly unusual coordination for c-type hemes, lysine and methionine as proximal ligands in NrfA and NrfH, respectively. The redox potential of the catalytic lysine-coordinated high spin heme of NrfA is -50 mV	
1.7.7.1	wild-type, to 1.25 A resolution and mutants Q448K, M175E, M175G, M175K to 2.0, 1.7. 1.7, 19 A resolution, respectively. The structure provides detailed geometries for the [4Fe–4S] cluster and the siroheme prosthetic groups