The binding of cofactors to photosystem I analyzed by spectroscopic and mutagenic methods

John H. Golbeck

Research output: Contribution to journalReview articlepeer-review

43 Scopus citations

Abstract

This review focuses on cofactor-ligand and protein-protein interactions within the photosystem I reaction center. The topics include a description of the electron transfer cofactors, the mode of binding of the cofactors to protein-bound ligands, and a description of intraprotein contacts that ultimately allow photosystem I to be assembled (in cyanobacteria) from 96 chlorophylls, 22 carotenoids, 2 phylloquinones, 3 [4Fe-4S] clusters, and 12 polypeptides. During the 15 years that have elapsed from the first report of crystals to the atomic-resolution X-ray crystal structure, cofactor-ligand interactions and protein-protein interactions were systematically being explored by spectroscopic and genetic methods. This article charts the interplay between these disciplines and assesses how good the early insights were in light of the current structure of photosystem I.

Original languageEnglish (US)
Pages (from-to)237-256
Number of pages20
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume32
DOIs
StatePublished - 2003

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology

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