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Literature summary for 1.7.2.1 extracted from

  • Hough, M.A.; Antonyuk, S.V.; Strange, R.W.; Eady, R.R.; Hasnain, S.S.
    Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase (2008), J. Mol. Biol., 378, 353-361.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
use of crystallography, together with online X-ray absorption spectroscopy and optical spectroscopy, to show that X-rays rapidly and selectively photoreduce the type 1 Cu centre, but that the type 2 Cu centre does not photoreduce directly over a typical crystallographic data collection time. Internal electron transfer between the type 1 Cu and type 2 Cu centres does not occur, and the type 2 Cu centre remains oxidized Achromobacter xylosoxidans

Organism

Organism UniProt Comment Textmining
Achromobacter xylosoxidans O68601
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Reaction

Reaction Comment Organism Reaction ID
nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ ordered mechanism in which electron transfer is gated by binding of nitrite to the type 2 Cu centre Achromobacter xylosoxidans