PetC1 Is the Major Rieske Iron-Sulfur Protein in the Cytochrome b6f Complex of Synechocystis sp. PCC 6803
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Dirk Schneider
- Stephan Berry
- Thomas Volkmer
- Andreas Seidler
- Matthias Rögner
- DOI
- 10.1074/jbc.m406288200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- Journal of Biological Chemistry
- Sprache
- en
- Paginierung
- 39383 - 39388
- Datum der Veröffentlichung
- 2004
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1074/jbc.m406288200
- Datum der Datenerfassung
- 2021
- Titel
- PetC1 Is the Major Rieske Iron-Sulfur Protein in the Cytochrome b6f Complex of Synechocystis sp. PCC 6803
- Ausgabe der Zeitschrift
- 279
Datenquelle: Crossref
- Andere Metadatenquellen:
-
- Abstract
- Many of the completely sequenced cyanobacterial genomes contain a gene family that encodes for putative Rieske iron-sulfur proteins. The Rieske protein is one of the large subunits of the cytochrome bc-type complexes involved in respiratory and photosynthetic electron transfer. In contrast to all other subunits of this complex that are encoded by single genes, the genome of the cyanobacterium Synechocystis PCC 6803 contains three petC genes, all encoding potential Rieske subunits. Most interestingly, any of the petC genes can be deleted individually without altering the Synechocystis phenotype dramatically. In contrast, double deletion experiments revealed that petC1 and petC2 cannot be deleted in combination, whereas petC3 can be deleted together with any of the other two petC genes. Further results suggest a different physiological function for each of the Rieske proteins. Whereas PetC2 can partly replace the dominating Rieske isoform PetC1, PetC3 is unable to functionally replace either PetC1 or PetC2 and may have a special function involving a special donor with a lower redox potential than plastoquinone. A predominant role of PetC1, which is (partly) different from PetC2, is suggested by the mutational analysis and a detailed characterization of the electron transfer reactions in the mutant strains.
- Addresses
- Lehrstuhl für Biochemie der Pflanzen, Ruhr-Universität Bochum, Germany. Dirk.Schneider@biochemie.uni-freiburg.de
- Autoren
- Dirk Schneider
- Stephan Berry
- Thomas Volkmer
- Andreas Seidler
- Matthias Rögner
- DOI
- 10.1074/jbc.m406288200
- eISSN
- 1083-351X
- Externe Identifier
- PubMed Identifier: 15262969
- Open access
- false
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- The Journal of biological chemistry
- Schlüsselwörter
- Cyanobacteria
- Chlorophyll
- Cytochrome b6f Complex
- Electron Transport Complex III
- Photosynthetic Reaction Center Complex Proteins
- Iron-Sulfur Proteins
- Mutagenesis, Insertional
- Photosynthesis
- Gene Deletion
- Electron Transport
- Oxidation-Reduction
- Open Reading Frames
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2004
- Paginierung
- 39383 - 39388
- Datum der Veröffentlichung
- 2004
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2004
- Titel
- PetC1 is the major Rieske iron-sulfur protein in the cytochrome b6f complex of Synechocystis sp. PCC 6803.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 279
Datenquelle: Europe PubMed Central
- Abstract
- Many of the completely sequenced cyanobacterial genomes contain a gene family that encodes for putative Rieske iron-sulfur proteins. The Rieske protein is one of the large subunits of the cytochrome bc-type complexes involved in respiratory and photosynthetic electron transfer. In contrast to all other subunits of this complex that are encoded by single genes, the genome of the cyanobacterium Synechocystis PCC 6803 contains three petC genes, all encoding potential Rieske subunits. Most interestingly, any of the petC genes can be deleted individually without altering the Synechocystis phenotype dramatically. In contrast, double deletion experiments revealed that petC1 and petC2 cannot be deleted in combination, whereas petC3 can be deleted together with any of the other two petC genes. Further results suggest a different physiological function for each of the Rieske proteins. Whereas PetC2 can partly replace the dominating Rieske isoform PetC1, PetC3 is unable to functionally replace either PetC1 or PetC2 and may have a special function involving a special donor with a lower redox potential than plastoquinone. A predominant role of PetC1, which is (partly) different from PetC2, is suggested by the mutational analysis and a detailed characterization of the electron transfer reactions in the mutant strains.
- Autoren
- Dirk Schneider
- Stephan Berry
- Thomas Volkmer
- Andreas Seidler
- Matthias Rögner
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/15262969
- DOI
- 10.1074/jbc.M406288200
- ISSN
- 0021-9258
- Ausgabe der Veröffentlichung
- 38
- Zeitschrift
- J Biol Chem
- Schlüsselwörter
- Chlorophyll
- Cyanobacteria
- Cytochrome b6f Complex
- Electron Transport
- Electron Transport Complex III
- Gene Deletion
- Iron-Sulfur Proteins
- Mutagenesis, Insertional
- Open Reading Frames
- Oxidation-Reduction
- Photosynthesis
- Photosynthetic Reaction Center Complex Proteins
- Sprache
- eng
- Country
- United States
- Paginierung
- 39383 - 39388
- PII
- S0021-9258(20)72736-5
- Datum der Veröffentlichung
- 2004
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2004
- Titel
- PetC1 is the major Rieske iron-sulfur protein in the cytochrome b6f complex of Synechocystis sp. PCC 6803.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 279
Datenquelle: PubMed
- Beziehungen:
- Eigentum von