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Prokaryotic assembly factors for the attachment of flavin to complex II.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2013 May; Vol. 1827 (5), pp. 637-47. Date of Electronic Publication: 2012 Sep 14. - Publication Year :
- 2013
-
Abstract
- Complex II (also known as Succinate dehydrogenase or Succinate-ubiquinone oxidoreductase) is an important respiratory enzyme that participates in both the tricarboxylic acid cycle and electron transport chain. Complex II consists of four subunits including a catalytic flavoprotein (SdhA), an iron-sulphur subunit (SdhB) and two hydrophobic membrane anchors (SdhC and SdhD). Complex II also contains a number of redox cofactors including haem, Fe-S clusters and FAD, which mediate electron transfer from succinate oxidation to the reduction of the mobile electron carrier ubiquinone. The flavin cofactor FAD is an important redox cofactor found in many proteins that participate in oxidation/reduction reactions. FAD is predominantly bound non-covalently to flavoproteins, with only a small percentage of flavoproteins, such as complex II, binding FAD covalently. Aside from a few examples, the mechanisms of flavin attachment have been a relatively unexplored area. This review will discuss the FAD cofactor and the mechanisms used by flavoproteins to covalently bind FAD. Particular focus is placed on the attachment of FAD to complex II with an emphasis on SdhE (a DUF339/SDH5 protein previously termed YgfY), the first protein identified as an assembly factor for FAD attachment to flavoproteins in prokaryotes. The molecular details of SdhE-dependent flavinylation of complex II are discussed and comparisons are made to known cofactor chaperones. Furthermore, an evolutionary hypothesis is proposed to explain the distribution of SdhE homologues in bacterial and eukaryotic species. Mechanisms for regulating SdhE function and how this may be linked to complex II function in different bacterial species are also discussed. This article is part of a Special Issue entitled: Respiratory complex II: Role in cellular physiology and disease.<br /> (Copyright © 2012 Elsevier B.V. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Bacteria genetics
Bacterial Proteins chemistry
Bacterial Proteins genetics
Electron Transport Complex II chemistry
Electron Transport Complex II genetics
Flavin-Adenine Dinucleotide chemistry
Models, Molecular
Molecular Sequence Data
Molecular Structure
Protein Binding
Protein Structure, Tertiary
Protein Subunits chemistry
Protein Subunits genetics
Protein Subunits metabolism
Sequence Homology, Amino Acid
Bacteria metabolism
Bacterial Proteins metabolism
Electron Transport Complex II metabolism
Flavin-Adenine Dinucleotide metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1827
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 22985599
- Full Text :
- https://doi.org/10.1016/j.bbabio.2012.09.003