Identification of the upper exciton component of the B850 bacteriochlorophylls of the LH2 antenna complex, using a B800-free mutant of Rhodobacter sphaeroides.

M.H.C. Koolhaas, R.N. Frese, G.J.S. Fowler, T.S. Bibby, S. Georgakopoulou, G. van der Zwan, C.N. Hunter, R. van Grondelle

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

In this paper, we report the circular dichroism (CD) spectra of two types of LH2 -only mutants of Rhodobacter sphaeroides. In the first, only the wild type LH2 is present, while in the second, the B800 binding site of LH2 has been either destabilized or removed. For the first time, we have identified a band in the CD spectrum of LH2, located at ~780 nm, that can be ascribed to the high exciton component of the B850 band. The experimental spectra have been modeled by theoretical calculations. On this basis, the average interaction strength between monomers in the B850 ring can be estimated to be approximately 300 cm
Original languageEnglish
Pages (from-to)4693-4698
JournalBiochemistry
Volume37
DOIs
Publication statusPublished - 1998

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