Heterogeneous Rieske Proteins in the Cytochrome b6 f Complex of Synechocystis PCC6803?
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Dirk Schneider
- Sven Skrzypczak
- Stefan Anemüller
- Christian L Schmidt
- Andreas Seidler
- Matthias Rögner
- DOI
- 10.1074/jbc.m104076200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 13
- Zeitschrift
- Journal of Biological Chemistry
- Sprache
- en
- Paginierung
- 10949 - 10954
- Datum der Veröffentlichung
- 2002
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1074/jbc.m104076200
- Datum der Datenerfassung
- 2021
- Titel
- Heterogeneous Rieske Proteins in the Cytochrome b6 f Complex of Synechocystis PCC6803?
- Ausgabe der Zeitschrift
- 277
Data source: Crossref
- Other metadata sources:
-
- Abstract
- The completely sequenced genome of the cyanobacterium Synechocystis PCC6803 contains three open reading frames, petC1, petC2, and petC3, encoding putative Rieske iron-sulfur proteins. After heterologous overexpression, all three gene products have been characterized and shown to be Rieske proteins as typified by sequence analysis and EPR spectroscopy. Two of the overproduced proteins contained already incorporated iron-sulfur clusters, whereas the third one formed unstable aggregates, in which the FeS cluster had to be reconstituted after refolding of the denatured protein. Although EPR spectroscopy showed typical FeS signals for all Rieske proteins, an unusual low midpoint potential was revealed for PetC3 by EPR redox titration. Detailed characterization of Synechocystis membranes indicated that all three Rieske proteins are expressed under physiological conditions. Both for PetC1 and PetC3 the association with the thylakoid membrane was shown, and both could be identified, although in different amounts, in the isolated cytochrome b(6)f complex. The considerably lower redox potential determined for PetC3 indicates heterogeneous cytochrome b(6)f complexes in Synechocystis and suggests still to be established alternative electron transport routes.
- Addresses
- Lehrstuhl für Biochemie der Pflanzen, Fakultät für Biologie, Ruhr-Universität Bochum, D-44780 Bochum, Germany.
- Autoren
- Dirk Schneider
- Sven Skrzypczak
- Stefan Anemüller
- Christian L Schmidt
- Andreas Seidler
- Matthias Rögner
- DOI
- 10.1074/jbc.m104076200
- eISSN
- 1083-351X
- Externe Identifier
- PubMed Identifier: 11788579
- Open access
- false
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 13
- Zeitschrift
- The Journal of biological chemistry
- Schlüsselwörter
- Cyanobacteria
- Cytochrome b6f Complex
- Electron Transport Complex III
- Cytochrome b Group
- Iron-Sulfur Proteins
- Electron Spin Resonance Spectroscopy
- Phylogeny
- Amino Acid Sequence
- Sequence Homology, Amino Acid
- Molecular Sequence Data
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2002
- Paginierung
- 10949 - 10954
- Datum der Veröffentlichung
- 2002
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2002
- Titel
- Heterogeneous Rieske proteins in the cytochrome b6f complex of Synechocystis PCC6803?
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 277
Data source: Europe PubMed Central
- Abstract
- The completely sequenced genome of the cyanobacterium Synechocystis PCC6803 contains three open reading frames, petC1, petC2, and petC3, encoding putative Rieske iron-sulfur proteins. After heterologous overexpression, all three gene products have been characterized and shown to be Rieske proteins as typified by sequence analysis and EPR spectroscopy. Two of the overproduced proteins contained already incorporated iron-sulfur clusters, whereas the third one formed unstable aggregates, in which the FeS cluster had to be reconstituted after refolding of the denatured protein. Although EPR spectroscopy showed typical FeS signals for all Rieske proteins, an unusual low midpoint potential was revealed for PetC3 by EPR redox titration. Detailed characterization of Synechocystis membranes indicated that all three Rieske proteins are expressed under physiological conditions. Both for PetC1 and PetC3 the association with the thylakoid membrane was shown, and both could be identified, although in different amounts, in the isolated cytochrome b(6)f complex. The considerably lower redox potential determined for PetC3 indicates heterogeneous cytochrome b(6)f complexes in Synechocystis and suggests still to be established alternative electron transport routes.
- Autoren
- Dirk Schneider
- Sven Skrzypczak
- Stefan Anemüller
- Christian L Schmidt
- Andreas Seidler
- Matthias Rögner
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/11788579
- DOI
- 10.1074/jbc.M104076200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 13
- Zeitschrift
- J Biol Chem
- Schlüsselwörter
- Amino Acid Sequence
- Cyanobacteria
- Cytochrome b Group
- Cytochrome b6f Complex
- Electron Spin Resonance Spectroscopy
- Electron Transport Complex III
- Iron-Sulfur Proteins
- Molecular Sequence Data
- Phylogeny
- Sequence Homology, Amino Acid
- Sprache
- eng
- Country
- United States
- Paginierung
- 10949 - 10954
- PII
- S0021-9258(18)52111-6
- Datum der Veröffentlichung
- 2002
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2002
- Titel
- Heterogeneous Rieske proteins in the cytochrome b6f complex of Synechocystis PCC6803?
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 277
Data source: PubMed
- Beziehungen:
- Property of