6ZUB
Cu nitrite reductase from Achromobacter cycloclastes: MSOX series at 170K, dose point 2
Summary for 6ZUB
| Entry DOI | 10.2210/pdb6zub/pdb |
| Descriptor | Copper-containing nitrite reductase, COPPER (II) ION, NITRITE ION, ... (6 entities in total) |
| Functional Keywords | cu nitrite reductase, nitrosyl, copper, msox, oxidoreductase |
| Biological source | Achromobacter cycloclastes |
| Total number of polymer chains | 1 |
| Total formula weight | 37134.61 |
| Authors | Hough, M.A.,Antonyuk, S.V.,Strange, R.W.,Hasnain, S.S. (deposition date: 2020-07-22, release date: 2021-06-23, Last modification date: 2024-01-31) |
| Primary citation | Hough, M.A.,Conradie, J.,Strange, R.W.,Antonyuk, S.V.,Eady, R.R.,Ghosh, A.,Hasnain, S.S. Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis. Chem Sci, 11:12485-12492, 2020 Cited by PubMed Abstract: The design and synthesis of copper complexes that can reduce nitrite to NO has attracted considerable interest. They have been guided by the structural information on the catalytic Cu centre of the widespread enzymes Cu nitrite reductases but the chemically novel side-on binding of NO observed in all crystallographic studies of these enzymes has been questioned in terms of its functional relevance. We show conversion of NO to NO in the crystal maintained at 170 K and present 'molecular movies' defining events during enzyme turnover including the formation of side-on Cu-NO intermediate. DFT modelling suggests that both {CuNO} and {CuNO} states may occur as side-on forms in an enzymatic active site with the stability of the {CuNO} side-on form governed by the protonation state of the histidine ligands. Formation of a copper-nitrosyl intermediate thus needs to be accommodated in future design templates for functional synthetic Cu-NiR complexes. PubMed: 34094452DOI: 10.1039/d0sc04797j PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.08 Å) |
Structure validation
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