NDUFB10

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 is an enzyme that in humans is encoded by the NDUFB10 gene.[5][6][7] NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 10 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.[8]

NDUFB10
Identifiers
Aliases	NDUFB10, PDSW, NADH:ubiquinone oxidoreductase subunit B10
External IDs	OMIM: 603843 MGI: 1915592 HomoloGene: 3343 GeneCards: NDUFB10
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 1,959,538 bp[1] End 1,961,975 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 A3.3 Start 24,722,060 bp[2] End 24,724,478 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • NADH dehydrogenase (ubiquinone) activity Cellular component • mitochondrial respiratory chain complex I • mitochondrion • electron transport • mitochondrial inner membrane • membrane Biological process • oxidation-reduction process • mitochondrial electron transport, NADH to ubiquinone • mitochondrial respiratory chain complex I assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4716	68342
Ensembl	ENSG00000140990	ENSMUSG00000040048
UniProt	O96000	Q9DCS9
RefSeq (mRNA)	NM_004548	NM_026684
RefSeq (protein)	NP_004539	NP_080960
Location (UCSC)	Chr 16: 1.96 – 1.96 Mb	Chr 17: 24.72 – 24.72 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Gene

The NDUFB10 gene is located on the p arm of chromosome 16 in position 13.3 and is 2,459 base pairs long.[9][10]

Structure

The NDUFB10 protein weighs 21 kDa and is composed of 172 amino acids.[9][10] NDUFB10 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site.[8] 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.[7]

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.[7] 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.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000140990 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040048 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Emahazion T, Beskow A, Gyllensten U, Brookes AJ (Nov 1998). "Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain". Cytogenetics and Cell Genetics. 82 (1–2): 115–9. doi:10.1159/000015082. PMID 9763677. S2CID 46818955.
6. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA (Dec 1998). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochemical and Biophysical Research Communications. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID 9878551.
7. "Entrez Gene: NDUFB10 NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 10, 22kDa".
8. Voet D, Voet JG, Pratt CW (2013). "Chapter 18". Fundamentals of biochemistry: life at the molecular level (4th ed.). Hoboken, NJ: Wiley. pp. 581–620. ISBN 978-0-470-54784-7.
9. Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
10. "NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).

Further reading

• Sheffler DJ, Kroeze WK, Garcia BG, Deutch AY, Hufeisen SJ, Leahy P, Brüning JC, Roth BL (Mar 2006). "p90 ribosomal S6 kinase 2 exerts a tonic brake on G protein-coupled receptor signaling". Proceedings of the National Academy of Sciences of the United States of America. 103 (12): 4717–22. Bibcode:2006PNAS..103.4717S. doi:10.1073/pnas.0600585103. PMC 1450237. PMID 16537434.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Yano M, Terada K, Mori M (Oct 2003). "AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins". The Journal of Cell Biology. 163 (1): 45–56. doi:10.1083/jcb.200305051. PMC 2173431. PMID 14557246.
• Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR (Feb 2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Human Molecular Genetics. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
• Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Oct 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.