NDUFB9 Recombinant Rabbit Monoclonal Antibody [JE63-09] (HA721015)

UNIPROT #

Q9Y6M9

PROTEIN NAME

NDUFB9

SYNONYMS

B22 antibody;CI B22 antibody;CI-B22 antibody;complex I B22 subunit antibody;Complex I-B22 antibody;DKFZp566O173 antibody;FLJ22885 antibody;I B22 antibody;LYR motif containing protein 3 antibody;LYR motif-containing protein 3 antibody;LYRM3 antibody;NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 9, 22kDa antibody;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 antibody;NADH ubiquinone oxidoreductase B22 subunit antibody;NADH-ubiquinone oxidoreductase B22 subunit antibody;NDUB9_HUMAN antibody;Ndufb9 antibody;UQOR22 antibody

SUBCELLULAR LOCATION

Mitochondrion inner membrane.

FUNCTION

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 is an enzyme that in humans is encoded by the NDUFB9 gene. NADH dehydrogenase (ubiquinone) 1 beta subcomplex subunit 9 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. 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. 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.