This is an old revision of this page, as edited by ProteinBoxBot(talk | contribs) at 05:41, 15 April 2016(Updating to new gene infobox populated via wikidata). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.
Revision as of 05:41, 15 April 2016 by ProteinBoxBot(talk | contribs)(Updating to new gene infobox populated via wikidata)
The NDUFB2 gene, located on the q arm of chromosome 7 in position 34, is 9,966 base pairs long and is composed of 4 exons.[7] The NDUFB2 protein weighs 8 kDa and is composed of 105 amino acids.[9][10] NDUFB2 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. 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.[8] NDUFB3 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. 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. Hydropathy analysis revealed that this subunit and 4 other subunits have an overall hydrophilic pattern, even though they are found within the hydrophobic protein (HP) fraction of complex I.[7]
Function
The human NDUFB2 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone.[7] However, NDUFB2 is an accessory subunit of the complex that is believed not to be involved in catalysis.[11] 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]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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". Cytogenet Cell Genet. 82 (1–2): 115–9. doi:10.1159/000015082. PMID9763677.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA (Jan 1999). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochem Biophys Res Commun. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID9878551.{{cite journal}}: CS1 maint: multiple names: authors list (link)
