Isolation of membrane protein subunits in their native state: evidence for selective binding of chlorophyll and carotenoid to the b6 subunit of the cytochrome b6f complex

Publication type:
Journal article
Metadata:
Autoren
  • Ute Boronowsky
  • Stephan-Olav Wenk
  • Dirk Schneider
  • Cornelia Jäger
  • Matthias Rögner
DOI
10.1016/s0005-2728(01)00184-0
ISSN
0005-2728
Ausgabe der Veröffentlichung
1
Zeitschrift
Biochimica et Biophysica Acta (BBA) - Bioenergetics
Sprache
en
Paginierung
55 - 66
Datum der Veröffentlichung
2001
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/s0005-2728(01)00184-0
Datum der Datenerfassung
2021
Titel
Isolation of membrane protein subunits in their native state: evidence for selective binding of chlorophyll and carotenoid to the b6 subunit of the cytochrome b6f complex
Ausgabe der Zeitschrift
1506

Data source: Crossref

Other metadata sources:
Abstract
Cytochrome (cyt) b-c complexes play a central role in electron transfer chains and are almost ubiquitous in nature. Although similar in their basic structure and function, the cyt b(6)f complex of photosynthetic membranes and its counterpart, the mitochondrial cyt bc(1) complex, show some characteristic differences which cannot be explained by the high resolution structure of the cyt bc(1) complex alone. Especially the presence of a chlorophyll molecule is a striking feature of all cyt b(6)f complex preparations described so far, imposing questions as to its structural and functional role. To allow a more detailed characterization, we here report the preparation of native subunits cyt b(6) and IV starting from a monomeric cyanobacterial cyt b(6)f complex. Spectroscopical and reversed-phase HPLC analyses of the purified cyt b(6) subunit showed that it contained not only two b-type hemes, but also one chlorophyll a molecule and a cyanobacterial carotenoid, echinenone. Evidence for selective binding of both pigments to this subunit is presented and their putative function is discussed.
Addresses
  • Plant Biochemistry, Faculty of Biology, Ruhr-Universität Bochum, Universitätsstrasse 150, D-44780, Bochum, Germany.
Autoren
  • U Boronowsky
  • S Wenk
  • D Schneider
  • C Jäger
  • M Rögner
DOI
10.1016/s0005-2728(01)00184-0
eISSN
1878-2434
Externe Identifier
  • PubMed Identifier: 11418097
Open access
false
ISSN
0006-3002
Ausgabe der Veröffentlichung
1
Zeitschrift
Biochimica et biophysica acta
Schlüsselwörter
  • Thylakoids
  • Cyanobacteria
  • Spinacia oleracea
  • Carotenoids
  • Chlorophyll
  • Cytochrome b6f Complex
  • Cytochrome b Group
  • Tryptophan
  • Peptides
  • Membrane Proteins
  • Detergents
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Spectrometry, Fluorescence
  • Spectrophotometry
  • Hydrogen-Ion Concentration
  • Solubility
  • Quaternary Ammonium Compounds
Sprache
eng
Medium
Print
Paginierung
55 - 66
Datum der Veröffentlichung
2001
Status
Published
Datum der Datenerfassung
2001
Titel
Isolation of membrane protein subunits in their native state: evidence for selective binding of chlorophyll and carotenoid to the b(6) subunit of the cytochrome b(6)f complex.
Sub types
  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
1506

Data source: Europe PubMed Central

Abstract
Cytochrome (cyt) b-c complexes play a central role in electron transfer chains and are almost ubiquitous in nature. Although similar in their basic structure and function, the cyt b(6)f complex of photosynthetic membranes and its counterpart, the mitochondrial cyt bc(1) complex, show some characteristic differences which cannot be explained by the high resolution structure of the cyt bc(1) complex alone. Especially the presence of a chlorophyll molecule is a striking feature of all cyt b(6)f complex preparations described so far, imposing questions as to its structural and functional role. To allow a more detailed characterization, we here report the preparation of native subunits cyt b(6) and IV starting from a monomeric cyanobacterial cyt b(6)f complex. Spectroscopical and reversed-phase HPLC analyses of the purified cyt b(6) subunit showed that it contained not only two b-type hemes, but also one chlorophyll a molecule and a cyanobacterial carotenoid, echinenone. Evidence for selective binding of both pigments to this subunit is presented and their putative function is discussed.
Autoren
  • U Boronowsky
  • S Wenk
  • D Schneider
  • C Jäger
  • M Rögner
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/11418097
DOI
10.1016/s0005-2728(01)00184-0
ISSN
0006-3002
Ausgabe der Veröffentlichung
1
Zeitschrift
Biochim Biophys Acta
Schlüsselwörter
  • Carotenoids
  • Chlorophyll
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Cyanobacteria
  • Cytochrome b Group
  • Cytochrome b6f Complex
  • Detergents
  • Hydrogen-Ion Concentration
  • Membrane Proteins
  • Peptides
  • Quaternary Ammonium Compounds
  • Solubility
  • Spectrometry, Fluorescence
  • Spectrophotometry
  • Spinacia oleracea
  • Thylakoids
  • Tryptophan
Sprache
eng
Country
Netherlands
Paginierung
55 - 66
PII
S0005272801001840
Datum der Veröffentlichung
2001
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2001
Titel
Isolation of membrane protein subunits in their native state: evidence for selective binding of chlorophyll and carotenoid to the b(6) subunit of the cytochrome b(6)f complex.
Sub types
  • Comparative Study
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
1506

Data source: PubMed

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