NADH dehydrogenase (quinone)
| NADH dehydrogenase (quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC no. | 1.6.99.5 | ||||||||
| CAS no. | 37256-36-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a NADH dehydrogenase (quinone) (EC 1.6.5.11) is an enzyme that catalyzes the chemical reaction
- NADH + H+ + a quinone NAD+ + a quinol
The 3 substrates of this enzyme are NADH, H+, and a quinone (electron acceptor), whereas its two products are NAD+ and a quinol (reduced acceptor).
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with other acceptors. The systematic name of this enzyme class is NADH:(quinone-acceptor) oxidoreductase. Other names in common use include reduced nicotinamide adenine dinucleotide (quinone) dehydrogenase, NADH-quinone oxidoreductase, NADH ubiquinone oxidoreductase, DPNH-menadione reductase, D-diaphorase, and NADH2 dehydrogenase (quinone), and mitochondrial (mt) complex I. This enzyme participates in oxidative phosphorylation. Several compounds are known to inhibit this enzyme, including AMP, and 2,4-dinitrophenol. NADH dehydrogenase is involved in the first step of the electron transport chain of oxidative phosphorylation (OXPHOS). Any change in the electron transport component caused by a mutation might effect the normal electron flow. This might be leading "an increase of bifurcation and generation of superoxidase radicals and increase oxidative stress in various types of cancer cells."[2]
In the electron transport chain NADH is mainly used to create a concentration gradient of hydrogen in order to make ATP. Since After NADH is oxidized a hydrogen is pumped out and NAD+ will be a product.[3]
Structural studies
Several structures are available of this enzyme, which is part of the respiratory chain. It is a multi-subunit enzyme in which this activity is located in the hydrophilic domain. The subunits of the membrane-embedded domain are responsible for proton translocation.
References
- ^ Berrisford JM, Sazanov LA (2009). "Structural basis for the mechanism of respiratory complex I". J Biol Chem. 284 (43): 29773–83. doi:10.1074/jbc.M109.032144. PMC 2785608. PMID 19635800.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Yusnita, Yakob; Norsiah, Md Desa; Rahman, A. Jamal (2010-12-01). "Mutations in mitochondrial NADH dehydrogenase subunit 1 (mtND1) gene in colorectal carcinoma". The Malaysian Journal of Pathology. 32 (2): 103–110. ISSN 0126-8635. PMID 21329181.
- ^ Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter (2002-01-01). "Electron-Transport Chains and Their Proton Pumps".
{{cite journal}}: Cite journal requires|journal=(help)
- Koli AK, Yearby C, Scott W, Donaldson KO (1969). "Purification and properties of three separate menadione reductases from hog liver". J. Biol. Chem. 244 (4): 621–9. PMID 4388793.
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