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1.13.11.49: chlorite O2-lyase

This is an abbreviated version!
For detailed information about chlorite O2-lyase, go to the full flat file.

Word Map on EC 1.13.11.49

Reaction

chloride
+
O2
=
Chlorite

Synonyms

chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.49 chlorite O2-lyase

Crystallization

Crystallization on EC 1.13.11.49 - chlorite O2-lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop method
-
thiocyanate inhibited enzyme with incorporated heme, crystals grown from well solution containing 100 mM Mes buffer (pH 5.5), 25% polyethylene glycol monomethyl ether 2000, 0.3 M KSCN, 5% glycerol, 160-260 mM (NH4)2SO4, before data collection crystals are soaked in a solution of the mother liquor including 16% glycerol, crystal is flash-frozen and kept at -173°C (100 K) for multiple anomalous dispersion (MAD) with synchrotron radiation
mutant enzymes Q74V and Q74E, sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5), 0.15 M MgSO4, 28% (w/v) polyethylene glycol 3350, and 3% (v/v) glycerol
recombinant protein, buffer-exchanged into 20 mM HEPES, pH 7.0, hanging-drop vapor diffusion, 16% PEG 8000, 0.2 M calcium acetate, 90 mM MES, pH 6.5, 293 K, chrystals appear after 2 h, co-crystals with substrate analogues sodium nitrite and sodium cyanide under same conditions
-
enzyme is a homopentamer, with presence of one b-type heme per monomer
in complex with thiocyanate and azide, to 0.976 and 1.0 A resolution, respectively. The crystal structure of the Cld-azide complex reveals a single well-defined orientation of the azide molecule in the heme pocket. EPR shows a pH-dependent heme structure, probably due to acid-base transitions of the surrounding amino-acid residues stabilizing azide
purified recombinant His-tagged enzyme, sitting-drop vapor diffusion technique and a nanodropdispensing robot, from 1.0 M Na2HPO4-NaH2PO4, pH 8.2, at 22°C, 1 week, X-ray diffraction structure determination and analysis at 2.10 A resolution
molecular dynamics simulations for binding of cyanide, chlorite, and hypochlorite with the enzyme in the ferrous, ferric, and compound I state. During reaction, a large portion of hypochlorite escapes from the heme cavity and enters the bulk phase. Leakage of hypochlorite in the mutant R173A is higher than that in the wild-type protein
purified recombinant His-tagged wild-type and mutant enzymes with bound cyanide, 22°C, sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.85-2.70 A resolution