Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.7.2.1 extracted from

  • Antonyuk, S.V.; Strange, R.W.; Sawers, G.; Eady, R.R.; Hasnain, S.S.
    Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism (2005), Proc. Natl. Acad. Sci. USA, 102, 12041-12046.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
atomic resolution structures of four forms of the green Cu-nitrite reductase: structure of the resting state of the enzyme at 0.9 A, structure of then nitrite-soaked complex at 1.10 A resolution, structure of the endogenously bound NO complex at 1.12-A resolution, structure of endogenously bound nitrite and NO in the same crystal at 1.15-A resolution Achromobacter cycloclastes

Organism

Organism UniProt Comment Textmining
Achromobacter cycloclastes P25006
-
-