Isolation and characterization of a major chlorophyll a c2 light-harvesting protein from a Chroomonas species (Cryptophyceae)

Katherine Ingram*, Roger G. Hiller

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Citations (Scopus)

Abstract

Three chlorophyll-protein complexes of a Chroomonas species (Cryptophyceae) have been separated by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The two bands at 100 and 42 kDa are Complex I (CP I) and Complex IV (CP IV), the ubiquitous chlorophyll a-proteins associated with Photosystems I and II, respectively. The third 55 kDa band, which had two peptide subunits (24 and 20 kDa), contained both chlorophyll a and chlorophyll c2 in a molar ratio of 1.4 chlorophyll a to 1 chlorophyll c2 ( chlorophyll a chlorophyll c2 ratio in whole cells = 4). A chlorophyll a c2 fraction with similar spectral and electrophoretic properties was isolated by digitonin-sucrose density gradient centrifugation. This fraction had no photochemical activity and contained only a single carotenoid species with absorbance maxima in methanol at 424, 448 and 476 nm. Efficient energy transfer from chlorophyll c2 to chlorophyll a occurred in the complex.

Original languageEnglish
Pages (from-to)310-319
Number of pages10
JournalBBA - Bioenergetics
Volume722
Issue number2
DOIs
Publication statusPublished - 17 Feb 1983

Keywords

  • (Cryptophyceae)
  • Chlorophyll c
  • Chlorophyll-protein
  • Fluorescence
  • Light-harvesting complex

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