ISOLATION AND CHARACTERIZATION OF A STRUCTURAL SUBUNIT FROM THE CORE LIGHT‐HARVESTING COMPLEX OF Rhodobacter sphaeroides 2.4.1 AND puc705‐BA

Mary C. Chang*, Leslye Meyer, Paul A. Loach

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Scopus citations

Abstract

Abstract— –A method for isolating a structural subunit, B825, from the B875 core light‐harvesting complex (LHC) of Rhodobacter sphaeroides 2.4.1 (wild‐type) and a B800‐B850(‐) mutant, puc705‐BA, is presented. This method, based on one developed to prepare a similar subunit, B820, from the core LHC of Rhodospirillum rubrum [Miller et al., Biochemistry 26, 5055–5062 (1987)], requires the dissociation of treated chromatophores with the detergent, octyl‐glucoside. A subsequent gel nitration step separates B800‐850 (if present), reaction centers, and free bacteriochlorophyll from the subunit complex. B825 was quantitatively reassociated into an 873 nm absorbing form which resembled the in vivo complex as judged by its absorption properties. The polypeptides in B825 and B800‐850 were isolated by HPLC and identified by N‐terminal amino acid sequencing. Two polypeptides, a and p, were found in each complex in a 1: 1 ratio. The spectral and biochemical properties of the subunits isolated from Rhodospirillum rubrum, Rhodobacter sphaeroides, and Rhodobacter capsulatus are compared.

Original languageEnglish (US)
Pages (from-to)873-881
Number of pages9
JournalPhotochemistry and Photobiology
Volume52
Issue number4
DOIs
StatePublished - Oct 1990

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry

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