Function and structure of complex II of the respiratory chain.
@article{Cecchini2003FunctionAS, title={Function and structure of complex II of the respiratory chain.}, author={Gary Cecchini}, journal={Annual review of biochemistry}, year={2003}, volume={72}, pages={ 77-109 } }
Complex II is the only membrane-bound component of the Krebs cycle and in addition functions as a member of the electron transport chain in mitochondria and in many bacteria. A recent X-ray structural solution of members of the complex II family of proteins has provided important insights into their function. One feature of the complex II structures is a linear electron transport chain that extends from the flavin and iron-sulfur redox cofactors in the membrane extrinsic domain to the quinone…
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References
SHOWING 1-10 OF 157 REFERENCES
Progress in understanding structure–function relationships in respiratory chain complex II
- Biology, ChemistryFEBS letters
- 2000
Structure and function of cytochrome bc complexes.
- Chemistry, BiologyAnnual review of biochemistry
- 2000
The cytochrome bc complexes represent a phylogenetically diverse group of complexes of electron-transferring membrane proteins, most familiarly represented by the mitochondrial and bacterial bc1…
Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex.
- Chemistry, BiologyCurrent opinion in structural biology
- 2000
The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane‐bound multisubunit hydrogenases
- BiologyFEBS letters
- 2000
Structure of the Escherichia coli fumarate reductase respiratory complex.
- Biology, ChemistryScience
- 1999
The crystal structure of intact fumarate reductase has been solved at 3.3 angstrom resolution and demonstrates that the cofactors are arranged in a nearly linear manner from the membrane-bound quinone to the active site flavin.
Iron-sulfur clusters/semiquinones in complex I.
- Biology, ChemistryBiochimica et biophysica acta
- 1998
Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice.
- Biology, ChemistryJournal of molecular biology
- 1998
The globular domain of bovine complex I is significantly bigger than that of the N. crassa enzyme, suggesting that the apparent additional subunit complexity of the bovines enzyme is associated with the globular part.
Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I).
- BiologyJournal of molecular biology
- 1998
It appears that the structural framework of procaryotic complex I is stabilized in eucaryotes by this additional mass, and a discrete location of additional protein in the peripheral arm of the mitochondrial complex is interpreted as being the possible position of two subunits with a specialized role in the biosynthesis of a yet unknown cofactor of complex I.
Succinate dehydrogenase and fumarate reductase from Escherichia coli.
- Biology, ChemistryBiochimica et biophysica acta
- 2002
Structures and proton-pumping strategies of mitochondrial respiratory enzymes.
- Physics, BiologyAnnual review of biophysics and biomolecular structure
- 2001
In this work, the strategies for performing proton pumping are described and the structural bases for the action of these proteins are discussed in light of recent crystal structures of several respiratory enzymes.