The major intrinsic light-harvesting protein of Amphidinium: characterization and relation to other light-harvesting proteins

Roger G. Hiller*, Pamela M. Wrench, Andrew P. Gooley, Grant Shoebridge, Jacques Breton

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)

Abstract

A major light‐harvesting complex (LHC) has been obtained from thylakoids of Amphidinium carterae solubilized with digitonin or decylmaltoside and separated by sucrose‐gradient centrifugation. The digitonin‐LHC forms a dark brown band at ‐17% sucrose and the decylmaltoside LHC one at ‐7% sucrose. Excellent energy transfer is retained from chlorophyll c and carotenoid to chlorophyll a. Absorbance and fluorescence excitation spectra show the existence of two major forms of chlorophyll c, one absorbing at 634 nm and the other at 649 nm. Linear dichroism spectra show the Qy transition of both forms of chlorophyll c to be aligned at <35° to the membrane plane. On sodium dodecylsulfate polyacrylamide gels the complex resolves as a single band of 19 kDa. A partial amino acid sequence shows the N‐terminus to be unblocked but modified; there is a persistent ambiguity of Ser/Asn at residue 4 and evidence for multiple but very similar polypeptides within the 19 kDa band. The peptide has strong identity with the N‐terminal regions of LHC from Phaeodactylum and Pavlova and LHC 1 of higher plants. Antibodies to the 19 kDa peptide react weakly with LHC of brown algae, diatoms and Prymnesiophytes but not with those of higher plants or Cryptophytes.

Original languageEnglish
Pages (from-to)125-131
Number of pages7
JournalPhotochemistry and Photobiology
Volume57
Issue number1
DOIs
Publication statusPublished - 1993

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