Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry

J Synchrotron Radiat. 2007 Jan;14(Pt 1):92-8. doi: 10.1107/S0909049506051259. Epub 2006 Dec 15.


X-ray exposure during crystallographic data collection can result in unintended redox changes in proteins containing functionally important redox centers. In order to directly monitor X-ray-derived redox changes in trapped oxidative half-reaction intermediates of Paracoccus denitrificans methylamine dehydrogenase, a commercially available single-crystal UV/Vis microspectrophotometer was installed on-line at the BioCARS beamline 14-BM-C at the Advanced Photon Source, Argonne, USA. Monitoring the redox state of the intermediates during X-ray exposure permitted the creation of a general multi-crystal data collection strategy to generate true structures of each redox intermediate.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / radiation effects*
  • Bacterial Proteins / ultrastructure
  • Dose-Response Relationship, Radiation
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / radiation effects
  • Multiprotein Complexes / ultrastructure
  • Oxidation-Reduction / radiation effects
  • Oxidoreductases Acting on CH-NH Group Donors / chemistry*
  • Oxidoreductases Acting on CH-NH Group Donors / radiation effects*
  • Oxidoreductases Acting on CH-NH Group Donors / ultrastructure
  • Paracoccus denitrificans / enzymology*
  • Protein Conformation / radiation effects
  • Radiation Dosage
  • Spectrophotometry, Ultraviolet / methods*
  • X-Rays


  • Bacterial Proteins
  • Multiprotein Complexes
  • mauC protein, Methylobacterium extorquens
  • methylamine dehydrogenase
  • Oxidoreductases Acting on CH-NH Group Donors