NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial (NADH-ubiquinone oxidoreductase ESSS subunit) is an enzyme that in humans is encoded by the NDUFB11gene.[1][2][3] NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 11 is an accessory subunit of the NADH dehydrogenase (ubiquinone) complex, located in the mitochondrial inner membrane. It is also known as Complex I and is the largest of the five complexes of the electron transport chain.[4]
The NDUFB11 gene is located on the p arm of chromosome X in position 11.23 and is 2,994 base pairs long.[5][6]
Protein
The NDUFB11 protein weighs 17 kDa and is composed of 153 amino acids.[5][6] NDUFB11 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes.
Structure
The structure is L-shaped with a long, hydrophobictransmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site.[4] It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.[3]
Function
The protein encoded by this gene is an accessory subunit of the multisubunit NADH:ubiquinone oxidoreductase (complex I) that is not directly involved in catalysis. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein complex has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified.[3] Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.[4]
References
↑Cui Y, Yu L, Gong R, Zhang M, Fan Y, Yue P, Zhao S (Jun 1999). "Cloning and tissue expressional characterization of a full-length cDNA encoding human neuronal protein P17.3". Biochemical Genetics. 37 (5–6): 175–85. doi:10.1023/A:1018734605214. PMID10544803.
↑Carroll J, Shannon RJ, Fearnley IM, Walker JE, Hirst J (Dec 2002). "Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits". The Journal of Biological Chemistry. 277 (52): 50311–7. doi:10.1074/jbc.M209166200. PMID12381726.
Petruzzella V, Tessa A, Torraco A, Fattori F, Dotti MT, Bruno C, Cardaioli E, Papa S, Federico A, Santorelli FM (Mar 2007). "The NDUFB11 gene is not a modifier in Leber hereditary optic neuropathy". Biochemical and Biophysical Research Communications. 355 (1): 181–7. doi:10.1016/j.bbrc.2007.01.140. PMID17292333.
