Multiple Step Assembly Of The Transmembrane Cytochrome b6

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • Carolin Dreher
  • Alexander Prodöhl
  • Ruth Hielscher
  • Petra Hellwig
  • Dirk Schneider
DOI
10.1016/j.jmb.2008.07.025
ISSN
0022-2836
Ausgabe der Veröffentlichung
4
Zeitschrift
Journal of Molecular Biology
Sprache
en
Paginierung
1057 - 1065
Datum der Veröffentlichung
2008
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.jmb.2008.07.025
Datum der Datenerfassung
2019
Titel
Multiple Step Assembly Of The Transmembrane Cytochrome b6
Ausgabe der Zeitschrift
382

Datenquelle: Crossref

Andere Metadatenquellen:
Abstract
We have analyzed the role of individual heme-ligating histidine residues for assembly of holo-cytochrome b(6), and we show that the two hemes b(L) and b(H) bind in two subsequent steps to the apo-protein. Binding of the low-potential heme b(L) is a prerequisite for binding the high-potential heme b(H). After substitution of His86, which serves as an axial ligand for heme b(L), the apo-protein did not bind heme, while substitution of the heme b(L)-ligating residue His187 still allowed binding of both hemes. Similarly, after replacement of His202, one axial ligand to heme b(H), binding of only heme b(L) was observed, whereas replacement of His100, the other heme b(H) ligand, resulted in binding of both hemes. These data indicate sequential heme binding during formation of the holo-cytochrome, and the two histidine residues, which serve as axial ligands to the same heme molecule (heme b(L) or heme b(H)), have different importance during heme binding and cytochrome assembly. Furthermore, determination of the heme midpoint potentials of the various cytochrome b(6) variants indicates a cooperative adjustment of the heme midpoint potentials in cytochrome b(6).
Addresses
  • Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Stefan-Meier-Strasse 17, 79104 Freiburg, Germany.
Autoren
  • Carolin Dreher
  • Alexander Prodöhl
  • Ruth Hielscher
  • Petra Hellwig
  • Dirk Schneider
DOI
10.1016/j.jmb.2008.07.025
eISSN
1089-8638
Externe Identifier
  • PubMed Identifier: 18656488
Open access
false
ISSN
0022-2836
Ausgabe der Veröffentlichung
4
Zeitschrift
Journal of molecular biology
Schlüsselwörter
  • Spinacia oleracea
  • Heme
  • Cytochromes b6
  • Histidine
  • Plant Proteins
  • Protein Isoforms
  • Recombinant Fusion Proteins
  • Protein Conformation
  • Protein Binding
  • Oxidation-Reduction
  • Models, Molecular
Sprache
eng
Medium
Print-Electronic
Online publication date
2008
Paginierung
1057 - 1065
Datum der Veröffentlichung
2008
Status
Published
Datum der Datenerfassung
2008
Titel
Multiple step assembly of the transmembrane cytochrome b6.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
382

Datenquelle: Europe PubMed Central

Abstract
We have analyzed the role of individual heme-ligating histidine residues for assembly of holo-cytochrome b(6), and we show that the two hemes b(L) and b(H) bind in two subsequent steps to the apo-protein. Binding of the low-potential heme b(L) is a prerequisite for binding the high-potential heme b(H). After substitution of His86, which serves as an axial ligand for heme b(L), the apo-protein did not bind heme, while substitution of the heme b(L)-ligating residue His187 still allowed binding of both hemes. Similarly, after replacement of His202, one axial ligand to heme b(H), binding of only heme b(L) was observed, whereas replacement of His100, the other heme b(H) ligand, resulted in binding of both hemes. These data indicate sequential heme binding during formation of the holo-cytochrome, and the two histidine residues, which serve as axial ligands to the same heme molecule (heme b(L) or heme b(H)), have different importance during heme binding and cytochrome assembly. Furthermore, determination of the heme midpoint potentials of the various cytochrome b(6) variants indicates a cooperative adjustment of the heme midpoint potentials in cytochrome b(6).
Date of acceptance
2008
Autoren
  • Carolin Dreher
  • Alexander Prodöhl
  • Ruth Hielscher
  • Petra Hellwig
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/18656488
DOI
10.1016/j.jmb.2008.07.025
eISSN
1089-8638
Ausgabe der Veröffentlichung
4
Zeitschrift
J Mol Biol
Schlüsselwörter
  • Cytochromes b6
  • Heme
  • Histidine
  • Models, Molecular
  • Oxidation-Reduction
  • Plant Proteins
  • Protein Binding
  • Protein Conformation
  • Protein Isoforms
  • Recombinant Fusion Proteins
  • Spinacia oleracea
Sprache
eng
Country
Netherlands
Paginierung
1057 - 1065
PII
S0022-2836(08)00867-X
Datum der Veröffentlichung
2008
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2008
Titel
Multiple step assembly of the transmembrane cytochrome b6.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
382

Datenquelle: PubMed

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