electron-transferring flavoprotein

WordNet

1. an elementary particle with negative charge (同)negatron
2. a globulin in blood plasma that carries iron (同)beta_globulin, siderophilin

PrepTutorEJDIC

1. 『電子』,エレクトロン

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/30 21:59:00」(JST)

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Electron transfer flavoprotein domain
electron transfer flavoprotein (etf) from paracoccus denitrificans
Identifiers
Symbol	ETF
Pfam	PF01012
Pfam clan	CL0039
InterPro	IPR014730
PROSITE	PDOC00583
SCOP	1efv
SUPERFAMILY	1efv
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Electron transfer flavoprotein FAD-binding domain
structure of electron transferring flavoprotein for methylophilus methylotrophus.
Identifiers
Symbol	ETF_alpha
Pfam	PF00766
Pfam clan	CL0085
InterPro	IPR014731
PROSITE	PDOC00583
SCOP	1efv
SUPERFAMILY	1efv
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

An electron transfer flavoprotein (ETF) or electron transfer flavoprotein complex (CETF) is a flavoprotein located on the matrix face of the inner mitochondrial membrane and functions as a specific electron acceptor for primary dehydrogenases, transferring the electrons to terminal respiratory systems such as electron-transferring-flavoprotein dehydrogenase. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by some prokaryotes under specific growth conditions, receiving electrons only from the oxidation of specific substrates (Group II).

ETFs are heterodimeric proteins composed of an alpha and beta subunit (ETFA and ETFB), and contain an FAD cofactor and AMP. ETF consists of three domains: domains I and II are formed by the N- and C-terminal portions of the alpha subunit, respectively, while domain III is formed by the beta subunit. Domains I and III share an almost identical alpha-beta-alpha sandwich fold, while domain II forms an alpha-beta-alpha sandwich similar to that of bacterial flavodoxins. FAD is bound in a cleft between domains II and III, while domain III binds the AMP molecule. Interactions between domains I and III stabilise the protein, forming a shallow bowl where domain II resides.

Mutation in ETFs can lead to deficiency of passing reducing equivalent of FADH₂ to electron transport chain, causing Glutaric acidemia type 2

See also

• Oxidative phosphorylation
• Electron transport chain
• Microbial metabolism
• Metabolism
• Glutaric acidemia type 2
• Electron-transferring-flavoprotein dehydrogenase

References

External links

• Pfam entry for Electron transfer flavoprotein domain
• Pfam entry for Electron transfer flavoprotein FAD-binding domain

UpToDate Contents

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English Journal

• A novel mode of lactate metabolism in strictly anaerobic bacteria.

• Weghoff MC1, Bertsch J, Müller V.
• Environmental microbiology.Environ Microbiol.2014 Apr 25. doi: 10.1111/1462-2920.12493. [Epub ahead of print]
• Lactate is a common substrate for major groups of strictly anaerobic bacteria but the biochemistry and bioenergetics of lactate oxidation is obscure. The high redox potential of the pyruvate/lactate pair of E0' = -190 mV excludes direct NAD+ reduction (E0' = -320 mV). To identify the hitherto unknow
• PMID 24762045

• PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling.

• Morais VA1, Haddad D, Craessaerts K, De Bock PJ, Swerts J, Vilain S, Aerts L, Overbergh L, Grünewald A, Seibler P, Klein C, Gevaert K, Verstreken P, De Strooper B.
• Science (New York, N.Y.).Science.2014 Apr 11;344(6180):203-7. doi: 10.1126/science.1249161. Epub 2014 Mar 20.
• Under resting conditions, Pink1 knockout cells and cells derived from patients with PINK1 mutations display a loss of mitochondrial complex I reductive activity, causing a decrease in the mitochondrial membrane potential. Analyzing the phosphoproteome of complex I in liver and brain from Pink1(-/-)
• PMID 24652937

Japanese Journal

• Decomposition of the fluorescence spectra of two FAD molecules in electron-transferring flavoprotein from Megasphaera elsdenii

• Sato Kyosuke,Nishina Yasuzo,Shiga Kiyoshi
• The journal of biochemistry 154(1), 61-66, 2013-07
• NAID 40019683313

• Interaction between NADH and electron-transferring flavoprotein from Megasphaera elsdenii

• Sato Kyosuke,Nishina Yasuzo,Shiga Kiyoshi
• The journal of biochemistry 153(6), 565-572, 2013-06
• NAID 40019655679

Related Links

• Electron-transferring flavoprotein - info | Homepage

An electron transfer flavoprotein (ETF) is a flavoprotein and functions as a specific electron acceptors for primary dehydrogenases, transferring the electrons ... ... An electron transfer flavoprotein (ETF) is a flavoprotein and functions as ...

• GO:0004174 electron-transferring-flavoprotein dehydrogenase ...

The European Bioinformatics Institute ... Database Code Database Name UniProtKB Universal Protein Knowledgebase UniProtKB/Swiss-Prot UniProtKB/Swiss-Prot UniProtKB/TrEMBL UniProtKB-TrEMBL protein sequence database

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★リンクテーブル★

リンク元	「電子伝達フラボタンパク」「電子伝達フラボタンパク質」「電子伝達フラボプロテイン」
関連記事	「flavoprotein」「electro」「electron」「transferrin」

「電子伝達フラボタンパク」

　　[★]

英

electron-transfer flavoprotein, electron-transferring flavoprotein, ETF

同

電子伝達フラボタンパク質

「電子伝達フラボタンパク質」

　　[★]

英

electron-transfer flavoprotein、electron-transferring flavoprotein

関

電子伝達フラボプロテイン

「電子伝達フラボプロテイン」

　　[★]

英

electron-transfer flavoprotein、electron-transferring flavoprotein

関

電子伝達フラボタンパク質

「flavoprotein」

　　[★]

• フラボタンパク質、フラボプロテイン、フラビンタンパク質

「electro」

　　[★]

• comb form.

• エレクトロ、電気

関

electric、electricity

「electron」

　　[★]

• n.

• 電子

関

electronic、fast electron、positron

　 　

「transferrin」

　　[★] トランスフェリン