Cecchini 2003 Annu Rev Biochem: Difference between revisions
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{{Publication | {{Publication | ||
|title=Cecchini G (2003) Function and structure of Complex II of the respiratory chain. Annu Rev Biochem 72:77-109. | |title=Cecchini G (2003) Function and structure of Complex II of the respiratory chain. Annu Rev Biochem 72:77-109. https://doi.org/10.1007/10.1146/annurev.biochem.72.121801.161700 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/14527321/ย PMID: 14527321] | |||
|authors=Cecchini G | |authors=Cecchini G | ||
|year=2003 | |year=2003 | ||
|journal=Annu Rev Biochem | |journal=Annu Rev Biochem | ||
|abstract=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 and b heme cofactors in the membrane domain. Exciting recent developments in relation to disease in humans and the formation of reactive oxygen species by complex II point to its overall importance in cellular physiology. | |||
|editor=Gnaiger E | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|preparations=Enzyme | |||
|enzymes=Complex II;succinate dehydrogenase | |||
|additional=BEC 2020.2 | |additional=BEC 2020.2 | ||
}} | }} | ||
== Cited by == | |||
{{Template:Cited by Gnaiger 2020 BEC MitoPathways}} |
Revision as of 23:40, 2 May 2023
Cecchini G (2003) Function and structure of Complex II of the respiratory chain. Annu Rev Biochem 72:77-109. https://doi.org/10.1007/10.1146/annurev.biochem.72.121801.161700 |
Cecchini G (2003) Annu Rev Biochem
Abstract: 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 and b heme cofactors in the membrane domain. Exciting recent developments in relation to disease in humans and the formation of reactive oxygen species by complex II point to its overall importance in cellular physiology.
โข Bioblast editor: Gnaiger E
Labels:
Preparation: Enzyme
Enzyme: Complex II;succinate dehydrogenase
BEC 2020.2
Cited by
- Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5th ed. Bioenerg Commun 2020.2. https://doi.org/10.26124/bec:2020-0002