Biliverdin reduction by cyanobacterial phycocyanobilin: ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates

Shih Long Tu, Alexander Gunn, Michael D. Toney, R. David Britt, J. Clark Lagarias

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

Cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the four electron reduction of biliverdin IXα (BV) to phycocyanobilin, a key step in the biosynthesis of the linear tetrapyrrole (bilin) prosthetic groups of cyanobacterial phytochromes and the light-harvesting phycobiliproteins. Using an anaerobic assay protocol, optically detected bilin-protein intermediates, produced during the PcyA catalytic cycle, were shown to correlate well with the appearance and decay of an isotropic g ≈ 2 EPR signal measured at low temperature. Absorption spectral simulations of biliverdin XIIIα reduction support a mechanism involving direct electron transfers from ferredoxin to protonated bilin:PcyA complexes.

Original languageEnglish (US)
Pages (from-to)8682-8693
Number of pages12
JournalJournal of the American Chemical Society
Volume126
Issue number28
DOIs
StatePublished - Jul 21 2004

ASJC Scopus subject areas

  • Chemistry(all)

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