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PMID: 2162198 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Photosynthetic reaction center of green sulfur bacteria studied by EPR.

Biochemistry ·Vol. 29 ·No. 16 ·1990-04-24 ·Pages 3834-42

Nitschke W, Feiler U, Rutherford AW

Abstract

Membrane preparations of two species of the green sulfur bacteria Chlorobium have been studied by EPR. Three signals were detected which were attributed to iron-sulfur centers acting as electron acceptors in the photosynthetic reaction center. (1) A signal from a center designated FB, (gz = 2.07, gy = 1.91, gx = 1.86) was photoinduced at 4 K. (2) A similar signal, FA (gz = 2.05, gy = 1.94, gx = 1.88), was photoinduced in addition to the FB signal upon a short period of illumination at 200 K. (3) Further illumination at 200 K resulted in the appearance of a broad feature at g = 1.78. This is attributed to the gx component of an iron-sulfur center designated FX. The designations of these signals as FB, FA, and FX are based on their spectroscopic similarities to signals in photosystem I (PS I). The orientation dependence of these EPR signals in ordered Chlorobium membrane multilayers is remarkably similar to that of their PS I homologues. A magnetic interaction between the reduced forms of FB and FA occurs, which is also very similar to that seen in PS I. However, in contrast to the situation in PS I, FA and FB cannot be chemically reduced by sodium dithionite at pH 11. This indicates redox potentials for FA and FB which are lower by at least 150 mV than their PS I counterparts. The triplet state of P840, the primary electron donor, could be photoinduced at 4 K in samples which had been preincubated with sodium dithionite and methyl viologen and then preilluminated at 200 K.(ABSTRACT TRUNCATED AT 250 WORDS)

MeSH Terms
Bacterial Proteins/analysis Cell Membrane/analysis Electron Spin Resonance Spectroscopy/methods Gram-Negative Chemolithotrophic Bacteria/analysis Iron/metabolism Models, Biological Oxidation-Reduction Photosynthetic Reaction Center Complex Proteins Temperature
Chemicals
Bacterial Proteins Photosynthetic Reaction Center Complex Proteins Iron
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nitschke W
Service de Biophysique, Département de Biologie, CEN Saclay, Gif sur Yvette, France.
Feiler U
Rutherford A W
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1990-04-24
Pages
3834-42
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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