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TitleSulfide oxidation in human sulfide quinone oxidoreductase is enthalpically driven: Contributions of the Lys-207 general base
Journal, issue, pagesTo Be Published
Publish dateJun 27, 2022 (structure data deposition date)
AuthorsBonanata, J. / Landry, A. / Ceric, K. / Ludlam, A. / Mascarenhas, R. / Coitino, L. / Banerjee, R.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-8dhk:
Crystal structure of human Sulfide Quinone Oxidoreductase K207E
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-MHA:
(CARBAMOYLMETHYL-CARBOXYMETHYL-AMINO)-ACETIC ACID / pH buffer*YM

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / K207E / FAD / Sulfide:quinone oxidoreductase / mitochondrial / trisulfide

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