Temperature and solvent effects on reaction centers from Chloroflexus aurantiacus and Chromatium tepidum.

Abstract:

:Temperature and solvent effects on reaction center structures were examined in two thermophilic photosynthetic bacteria, Chloroflexus aurantiacus and Chromatium tepidum, in order to gain insight into the interactions among the reaction center proteins and pigment systems. Thermal stability of the reaction centers was found to be proportional to the optimum growth temperature. Circular dichroism (CD) spectra in the 250-300 nm region indicated that thermal denaturation destroyed tertiary structures (helix-to-helix interactions or amino acid residue conformation) in the native reaction center, keeping helical structures intact. Absorption and circular dichroism spectral changes showed that alcohol denatured the so-called special pair and the accessory BChl a independently. The alcohol denaturation further indicates that the coordination between BChl a and amino acid residue in the protein is one of the important interactions maintaining the pigment organization of the reaction centers.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Nozawa T,Madigan MT

doi

10.1093/oxfordjournals.jbchem.a123624

subject

Has Abstract

pub_date

1991-10-01 00:00:00

pages

588-94

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

110

pub_type

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