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Literature summary for 1.7.2.1 extracted from

  • Oganesyan, V.S.; Cheesman, M.R.; Thomson, A.J.
    Magnetic circular dichroism evidence for a weakly coupled heme-radical pair at the active site of cytochrome cd1, a nitrite reductase (2007), Inorg. Chem., 46, 10950-10952.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron in hemes c and d1, the cytochrome cd1 heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, FeIII heme d1 [d1(FeIII)] is bound by histidine and tyrosine, structure, overview Paracoccus pantotrophus

Organism

Organism UniProt Comment Textmining
Paracoccus pantotrophus P72181
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-

Synonyms

Synonyms Comment Organism
cytochrome cd1 nitrite reductase
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Paracoccus pantotrophus
nitrite reductase
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Paracoccus pantotrophus

Cofactor

Cofactor Comment Organism Structure
cytochrome cd1 the heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, binding structure, overview Paracoccus pantotrophus
heme heme c has bis-histidine ligation and FeIII heme d1 [d1(FeIII)] is bound by histidine and tyrosine. The cytochrome cd1 heme d1 is not in the oxoferryl (FeIVdO) state but is low-spin FeIII weakly coupled to a radical species, structure, overview Paracoccus pantotrophus