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TitleActivation of redox tyrosine switch is required for ligand binding at the catalytic site in heme-cu nitrite reductases
Journal, issue, pagesTo be published
Publish dateJun 28, 2017 (structure data deposition date)
AuthorsDong, J. / Sasaki, D. / Eady, R. / Antonyuk, S.V. / Hasnain, S.S.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.78 - 2.2 Å
Structure data

PDB-5obo:
Crystal structure of nitrite bound D97N mutant of three-domain heme-Cu nitrite reductase from Ralstonia pickettii
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-5ocb:
Crystal structure of nitric oxide bound D97N mutant of three-domain heme-Cu nitrite reductase from Ralstonia pickettii
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

PDB-5ocf:
Crystal structure of nitric oxide bound to three-domain heme-Cu nitrite reductase from Ralstonia pickettii
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-6fja:
Crystal structure of T2D three-domain heme-Cu nitrite reductase from Ralstonia pickettii
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-HEC:
HEME C

ChemComp-GOL:
GLYCEROL

ChemComp-NO2:
NITRITE ION

ChemComp-HOH:
WATER

ChemComp-NO:
NITRIC OXIDE

Source
  • ralstonia sp. 5_2_56faa (bacteria)
  • ralstonia pickettii (bacteria)
KeywordsELECTRON TRANSPORT / nitrite reductase / electron transfer / redox reactions / tyrosine activation

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