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Literature summary extracted from

  • Stein, N.; Love, D.; Judd, E.T.; Elliott, S.J.; Bennett, B.; Pacheco, A.A.
    Correlations between the electronic properties of Shewanella oneidensis cytochrome c nitrite reductase (ccNiR) and its structure effects of heme oxidation state and active site ligation (2015), Biochemistry, 54, 3749-3758 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.2.2 UV/Vis spectropotentiometric results yield highly reproducible values for the heme midpoint potentials, which can be assigned to specific hemes in each protomer. Addition of the strong-field ligand cyanide leads to a 70 mV positive shift of the active site's midpoint potential, the cyanide binds to the initially 5-coordinate high-spin heme and triggers a high-spin to low-spin transition. With cyanide present three of the remaining hemes give rise to distinctive and readily assignable EPR spectral changes upon reduction Shewanella oneidensis

Protein Variants

EC Number Protein Variants Comment Organism
1.7.2.2 H268M one of the EPR-silent heme's histidine axial ligands is replaced with a methionine Shewanella oneidensis

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.2 Shewanella oneidensis Q8EAC7
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Synonyms

EC Number Synonyms Comment Organism
1.7.2.2 NrfA
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 Shewanella oneidensis