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Results 1 - 6 of 6
EC Number Crystallization (Commentary)
Show all pathways known for 1.7.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.7.7.1modeling of structure based on spinach nitrite reductase. Arginine and lysine residues are involved in electrostatically-stabilized binding to ferredoxin
Show all pathways known for 1.7.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.7.7.1NMR-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
Show all pathways known for 1.7.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.7.7.1sitting drop vapour diffusion method
Show all pathways known for 1.7.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.7.7.1the 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
Show all pathways known for 1.7.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.7.7.1the 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
Show all pathways known for 1.7.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.7.7.1wild-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
Results 1 - 6 of 6