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

Arwen R. Pearson, Reinhard Pahl, Elena G. Kovaleva, Victor L. Davidson, Carrie M. Wilmot

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)92-98
Number of pages7
JournalJournal of Synchrotron Radiation
Volume14
Issue number1
DOIs
StatePublished - Jan 2007

Keywords

  • Methylamine dehydrogenase
  • Reaction intermediates
  • Single-crystal microspectrophotometry
  • Structural enzymology
  • Tryptophan tryptophylquinone

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