Literature summary for 1.7.2.2 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 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Organism

Organism	UniProt	Comment	Textmining
Shewanella oneidensis	Q8EAC7	-	-

Synonyms

Synonyms	Comment	Organism
NrfA	-	Shewanella oneidensis

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Release 2023.1 (January 2023)