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Literature summary for 1.7.7.1 extracted from

  • Todorovic, S.; Rodrigues, M.; Matos, D.; Pereira, I.
    Redox properties of lysine- and methionine-coordinated hemes ensure downhill electron transfer in NrfH 2A 4 nitrite reductase (2012), J. Phys. Chem. B, 116, 5637-5643.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Desulfovibrio vulgaris
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 Desulfovibrio vulgaris

Organism

Organism UniProt Comment Textmining
Desulfovibrio vulgaris
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Desulfovibrio vulgaris Q72EF3 catalytic subunit NrfA
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Synonyms

Synonyms Comment Organism
NrfA
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Desulfovibrio vulgaris
NrfH
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Desulfovibrio vulgaris