Heme Binding Constricts the Conformational Dynamics of the Cytochrome b559′ Heme Binding Cavity
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Yasar Akdogan
- Veerappan Anbazhagan
- Dariush Hinderberger
- Dirk Schneider
- DOI
- 10.1021/bi300489s
- eISSN
- 1520-4995
- ISSN
- 0006-2960
- Ausgabe der Veröffentlichung
- 36
- Zeitschrift
- Biochemistry
- Sprache
- en
- Online publication date
- 2012
- Paginierung
- 7149 - 7156
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Herausgeber
- American Chemical Society (ACS)
- Herausgeber URL
- http://dx.doi.org/10.1021/bi300489s
- Datum der Datenerfassung
- 2023
- Titel
- Heme Binding Constricts the Conformational Dynamics of the Cytochrome <i>b</i><sub>559</sub>′ Heme Binding Cavity
- Ausgabe der Zeitschrift
- 51
Data source: Crossref
- Other metadata sources:
-
- Abstract
- Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. The PsbF polypeptide can dimerize in the absence and presence of heme. To monitor structural alterations associated with binding of heme to the apo-cytochrome, we analyzed the apo- and holo-cytochrome structure by electron paramagnetic resonance spectroscopy. Spin labeling of amino acids located close to the heme binding domain of the cytochrome revealed that the structure of the heme binding domain is unconstrained in the absence of heme. Heme binding restricts the conformational dynamics of the heme binding domain, resulting in the structurally more constricted holo-cytochrome structure.
- Addresses
- Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany.
- Autoren
- Yasar Akdogan
- Veerappan Anbazhagan
- Dariush Hinderberger
- Dirk Schneider
- DOI
- 10.1021/bi300489s
- eISSN
- 1520-4995
- Externe Identifier
- PubMed Identifier: 22897206
- Open access
- false
- ISSN
- 0006-2960
- Ausgabe der Veröffentlichung
- 36
- Zeitschrift
- Biochemistry
- Schlüsselwörter
- Cell Membrane
- Spin Labels
- Heme
- Photosystem II Protein Complex
- Cytochrome b Group
- Peptides
- Apoenzymes
- Electron Spin Resonance Spectroscopy
- Temperature
- Amino Acid Sequence
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Protein Binding
- Models, Molecular
- Molecular Sequence Data
- Glycophorins
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2012
- Paginierung
- 7149 - 7156
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Datum der Datenerfassung
- 2012
- Titel
- Heme binding constricts the conformational dynamics of the cytochrome b(559)' heme binding cavity.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 51
Data source: Europe PubMed Central
- Abstract
- Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. The PsbF polypeptide can dimerize in the absence and presence of heme. To monitor structural alterations associated with binding of heme to the apo-cytochrome, we analyzed the apo- and holo-cytochrome structure by electron paramagnetic resonance spectroscopy. Spin labeling of amino acids located close to the heme binding domain of the cytochrome revealed that the structure of the heme binding domain is unconstrained in the absence of heme. Heme binding restricts the conformational dynamics of the heme binding domain, resulting in the structurally more constricted holo-cytochrome structure.
- Autoren
- Yasar Akdogan
- Veerappan Anbazhagan
- Dariush Hinderberger
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/22897206
- DOI
- 10.1021/bi300489s
- eISSN
- 1520-4995
- Ausgabe der Veröffentlichung
- 36
- Zeitschrift
- Biochemistry
- Schlüsselwörter
- Amino Acid Sequence
- Apoenzymes
- Cell Membrane
- Cytochrome b Group
- Electron Spin Resonance Spectroscopy
- Glycophorins
- Heme
- Models, Molecular
- Molecular Sequence Data
- Peptides
- Photosystem II Protein Complex
- Protein Binding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Spin Labels
- Temperature
- Sprache
- eng
- Country
- United States
- Paginierung
- 7149 - 7156
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2012
- Titel
- Heme binding constricts the conformational dynamics of the cytochrome b(559)' heme binding cavity.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 51
Data source: PubMed
- Beziehungen:
- Property of