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S. cerevisiae COX1

Saccharomyces cerevisiae is a species of yeast. It has been instrumental to winemaking, baking, and brewing since ancient times.
Full Name
Saccharomyces Cerevisiae Cytochrome C Oxidase Subunit 1
Function
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX1 is a catalytic core subunit containing heme A and the active site BNC with heme A3 and the copper atom CU(B) (PubMed:30598554).
Biological Process
Biological Process aerobic respirationManual Assertion Based On ExperimentIMP:SGD
Biological Process cellular respirationManual Assertion Based On ExperimentIDA:ComplexPortal
Biological Process electron transport coupled proton transportManual Assertion Based On ExperimentIBA:GO_Central
Biological Process mitochondrial electron transport, cytochrome c to oxygenManual Assertion Based On ExperimentIDA:SGD
Biological Process respiratory electron transport chainManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Mitochondrion inner membrane
Topology
Mitochondrial matrix: 1-14
Helical: 15-39
Mitochondrial intermembrane: 40-54
Helical: 55-88
Mitochondrial matrix: 89-97
Helical: 98-118
Mitochondrial intermembrane: 119-142
Helical: 143-171
Mitochondrial matrix: 172-183
Helical: 184-215
Mitochondrial intermembrane: 216-228
Helical: 229-263
Mitochondrial matrix: 264-269
Helical: 270-295
Mitochondrial intermembrane: 296-298
Helical: 299-327
Mitochondrial matrix: 328-335
Helical: 336-358
Mitochondrial intermembrane: 359-370
Helical: 371-400
Mitochondrial matrix: 401-406
Helical: 407-431
Mitochondrial intermembrane: 432-449
Helical: 450-474
Mitochondrial matrix: 475-534
PTM
The N-terminus is blocked.

Anti-S. cerevisiae COX1 antibodies

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Target: S. cerevisiae COX1
Host: Mouse
Antibody Isotype: IgG2b
Specificity: S. cerevisiae
Clone: CBMW-H1377
Application*: WB
For Research Use Only. Not For Clinical Use.
(P): Predicted
* Abbreviations
IFImmunofluorescence
IHImmunohistochemistry
IPImmunoprecipitation
WBWestern Blot
EELISA
MMicroarray
CIChromatin Immunoprecipitation
FFlow Cytometry
FNFunction Assay
IDImmunodiffusion
RRadioimmunoassay
TCTissue Culture
GSGel Supershift
NNeutralization
BBlocking
AActivation
IInhibition
DDepletion
ESELISpot
DBDot Blot
MCMass Cytometry/CyTOF
CTCytotoxicity
SStimulation
AGAgonist
APApoptosis
IMImmunomicroscopy
BABioassay
CSCostimulation
EMElectron Microscopy
IEImmunoelectrophoresis
PAPeptide Array
ICImmunocytochemistry
PEPeptide ELISA
MDMeDIP
SHIn situ hybridization
IAEnzyme Immunoassay
SEsandwich ELISA
PLProximity Ligation Assay
ECELISA(Cap)
EDELISA(Det)
BIBioimaging
IOImmunoassay
LFLateral Flow Immunoassay
LALuminex Assay
CImmunohistochemistry-Frozen Sections
PImmunohistologyp-Paraffin Sections
ISIntracellular Staining for Flow Cytometry
MSElectrophoretic Mobility Shift Assay
RIRNA Binding Protein Immunoprecipitation (RIP)
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