Characterization of two cytochrome b 6 proteins from the cyanobacterium Gloeobacter violaceus PCC 7421

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • Carolin Dreher
  • Ruth Hielscher
  • Alexander Prodöhl
  • Petra Hellwig
  • Dirk Schneider
DOI
10.1007/s10863-010-9279-6
eISSN
1573-6881
ISSN
0145-479X
Ausgabe der Veröffentlichung
6
Zeitschrift
Journal of Bioenergetics and Biomembranes
Sprache
en
Online publication date
2010
Paginierung
517 - 526
Datum der Veröffentlichung
2010
Status
Published
Herausgeber
Springer Science and Business Media LLC
Herausgeber URL
http://dx.doi.org/10.1007/s10863-010-9279-6
Datum der Datenerfassung
2021
Titel
Characterization of two cytochrome b 6 proteins from the cyanobacterium Gloeobacter violaceus PCC 7421
Ausgabe der Zeitschrift
42

Datenquelle: Crossref

Andere Metadatenquellen:
Abstract
In the genome of the untypical cyanobacterium Gloeobacter violaceus PCC 7421 two potential cytochrome b (6) proteins PetB1 and PetB2 are encoded. Such a situation has not been observed in cyanobacteria, algae and higher plants before, and both proteins are not characterized at all yet. Here, we show that both apo-proteins bind heme with high affinity and the spectroscopic characteristics of both holo-proteins are distinctive for cytochrome b (6) proteins. However, while in PetB2 one histidine residue, which corresponds to H100 and serves as an axial ligand for heme b (H) in PetB1, is mutated, both PetB proteins bind two heme molecules with different midpoint potentials. To recreate the canonical heme b (H) binding cavity in PetB2 we introduced a histidine residue at the position corresponding to H100 in PetB1 and subsequently characterized the generated protein variant. The presented data indicate that two bona fide cytochrome b (6) proteins are encoded in Gloeobacter violaceus. Furthermore, the two petB genes of Gloeobacter violaceus are each organized in an operon together with a petD gene. Potential causes and consequences of the petB and petD gene heterogeneity are discussed.
Addresses
  • Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität Freiburg, 79104, Freiburg, Germany.
Autoren
  • Carolin Dreher
  • Ruth Hielscher
  • Alexander Prodöhl
  • Petra Hellwig
  • Dirk Schneider
DOI
10.1007/s10863-010-9279-6
eISSN
1573-6881
Externe Identifier
  • PubMed Identifier: 20237831
Open access
false
ISSN
0145-479X
Ausgabe der Veröffentlichung
6
Zeitschrift
Journal of bioenergetics and biomembranes
Schlüsselwörter
  • Cyanobacteria
  • Heme
  • Cytochrome b6f Complex
  • Cytochromes b6
  • Electrophoresis, Polyacrylamide Gel
  • Sequence Alignment
  • Mutagenesis
  • Amino Acid Sequence
  • Operon
  • Molecular Sequence Data
Sprache
eng
Medium
Print-Electronic
Online publication date
2010
Paginierung
517 - 526
Datum der Veröffentlichung
2010
Status
Published
Datum der Datenerfassung
2010
Titel
Characterization of two cytochrome b6 proteins from the cyanobacterium Gloeobacter violaceus PCC 7421.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
42

Datenquelle: Europe PubMed Central

Abstract
In the genome of the untypical cyanobacterium Gloeobacter violaceus PCC 7421 two potential cytochrome b (6) proteins PetB1 and PetB2 are encoded. Such a situation has not been observed in cyanobacteria, algae and higher plants before, and both proteins are not characterized at all yet. Here, we show that both apo-proteins bind heme with high affinity and the spectroscopic characteristics of both holo-proteins are distinctive for cytochrome b (6) proteins. However, while in PetB2 one histidine residue, which corresponds to H100 and serves as an axial ligand for heme b (H) in PetB1, is mutated, both PetB proteins bind two heme molecules with different midpoint potentials. To recreate the canonical heme b (H) binding cavity in PetB2 we introduced a histidine residue at the position corresponding to H100 in PetB1 and subsequently characterized the generated protein variant. The presented data indicate that two bona fide cytochrome b (6) proteins are encoded in Gloeobacter violaceus. Furthermore, the two petB genes of Gloeobacter violaceus are each organized in an operon together with a petD gene. Potential causes and consequences of the petB and petD gene heterogeneity are discussed.
Date of acceptance
2010
Autoren
  • Carolin Dreher
  • Ruth Hielscher
  • Alexander Prodöhl
  • Petra Hellwig
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/20237831
DOI
10.1007/s10863-010-9279-6
eISSN
1573-6881
Ausgabe der Veröffentlichung
6
Zeitschrift
J Bioenerg Biomembr
Schlüsselwörter
  • Amino Acid Sequence
  • Cyanobacteria
  • Cytochrome b6f Complex
  • Cytochromes b6
  • Electrophoresis, Polyacrylamide Gel
  • Heme
  • Molecular Sequence Data
  • Mutagenesis
  • Operon
  • Sequence Alignment
Sprache
eng
Country
United States
Paginierung
517 - 526
Datum der Veröffentlichung
2010
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2011
Titel
Characterization of two cytochrome b6 proteins from the cyanobacterium Gloeobacter violaceus PCC 7421.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
42

Datenquelle: PubMed

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