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TitleConformational rigidity of cytochrome c'-alpha from a thermophile is associated with slow NO binding.
Journal, issue, pagesBiophys. J., Vol. 123, Page 2594-2603, Year 2024
Publish dateDec 27, 2023 (structure data deposition date)
AuthorsFujii, S. / Wilson, M.T. / Adams, H.R. / Mikolajek, H. / Svistunenko, D.A. / Smyth, P. / Andrew, C.R. / Sambongi, Y. / Hough, M.A.
External linksBiophys. J. / PubMed:38937973
MethodsX-ray diffraction
Resolution1.63 Å
Structure data

PDB-8rkp:
Cytochrome c prime from Hydrogenophilus thermoluteolus: Ferrous recombinant native with bound NO
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

Chemicals

ChemComp-NO:
NITRIC OXIDE

ChemComp-ASC:
ASCORBIC ACID / medication*YM

ChemComp-HEC:
HEME C

ChemComp-HOH:
WATER

Source
  • hydrogenophilus thermoluteolus (bacteria)
KeywordsELECTRON TRANSPORT / Nitrix oxide binding / Heme protein

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