Anti-MTCO1/mt-Co1 Antibody Picoband® Fluoro550 Conjugated

Cytochrome c oxidase subunit I (CO1 or MTCO1) is 1 of 3 mitochondrial DNA (mtDNA) encoded subunits (MTCO1, MTCO2, MTCO3) of respiratory Complex IV. Complex IV is located within the mitochondrial inner membrane and is the third and final enzyme of the electron transport chain of mitochondrial oxidative phosphorylation. It is composed of 13 polypeptides. Subunits I, II, and III (MTCO1, MTCO2, MTCO3) are encoded by mtDNA while subunits IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, and VIII are nuclear encoded. The cytochrome c oxidase family of enzymes have 4 redox centers, 2 hemes and 2 copper centers. In mitochondrial Complex IV, the 2 hemes are a and a3 and the 2 coppers are CuA and CuB. The 2 hemes and CuB are bound to subunit I. Acin-Perez et al. (2003) identified a cell line containing single and double missense mutations in the cytochrome c oxidase (COX) subunit I gene of mouse mitochondrial DNA. And they hypothesized that deleterious mutations can arise and become predominant; cultured cells can maintain several mtDNA haplotypes at stable frequencies; the respiratory chain has little spare COX capacity; and that the size of a cavity in the vicinity of val421 in MTCO1I of animal COX may affect the function of the enzyme.

Cancer, Cancer Metabolism, Energy Transfer Pathways, Integration Of Energy, Integration Of Energy Metabolism, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Mitochondria, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Organelles, Oxidative Phosphorylation, Pathways and Processes, Signal Transduction, Subcellular Markers, Tags & Cell Markers

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

1. Kadenbach, B.; Jarausch, J.; Hartmann, R.; Merle, P. : Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoretic procedure. Anal. Biochem. 129: 517-521, 1983. 2. Shoffner, J. M.; Wallace, D. C. : Oxidative phosphorylation diseases.In: Scriver, C. R.; Beaudet, A. L.; Sly, W. S.; Valle, D. (eds.) : The Metabolic and Molecular Bases of Inherited Disease. Vol. 1. New York: McGraw-Hill (7th ed.) 1995. Pp. 1535-1609. 3. Hosler, J. P.; Ferguson-Miller, S.; Calhoun, M. W.; Thomas, J. W.; Hill, J.; Lemieux, L.; Ma, J.; Georgiou, C.; Fetter, J.; Shapleigh, J.; Tecklenburg, M. M. J.; Babcock, G. T.; Gennis, R. B. : Insight into the active-site structure and function of cytochrome oxidase by analysis of site-ed mutants of bacterial cytochrome aa3 and cytochrome bo. J. Bioenerg. Biomembr. 25: 121-136, 1993. 4. Acin-Perez, R.; Bayona-Bafaluy, M. P.; Bueno, M.; Machicado, C.; Fernandez-Silva, P.; Perez-Martos, A.; Montoya, J.; Lopez-Perez, M. J.; Sancho, J.; Enriquez, J. A. : An intragenic suppressor in the cytochrome c oxidase I gene of mouse mitochondrial DNA. Hum. Molec. Genet. 12: 329-339, 2003.