Type | Description |
---|---|
Definition | cytochrome c oxidase subunit I |
Date | Results | Publications |
---|---|---|
2020-04-11 12:32:00 | structural analysis of the formation of monomeric CcO, dimeric CcO, and supercomplex, as well as their role in regulation of CcO activity | 31533957 |
2019-05-04 10:18:00 | By using time-resolved serial femtosecond crystallography, we identified a key oxygen intermediate of bovine Cytochrome c oxidase (CcO) | 30808749 |
2018-09-29 10:16:00 | Therefore the data do not support the proposal that the inhibitory effect of Ca(2+) on CcO activity may be explained by the Ca(2+)-induced shift of Em of heme a. Rather, Ca(2+) retards electron transfer by inhibition of charge dislocation in the exit part of the proton channel H in mammalian CcO, that is absent in the bacterial oxidases. | 29635042 |
2014-06-21 13:07:00 | Ca(2+)- binding at the Cation Binding Site is proposed to inhibit proton-transfer through the exit part of the proton conducting pathway H in the mammalian oxidases. | 24058566 |
2011-11-05 10:29:00 | ovine heart cytochrome c oxidase, the prototype of the mammalian enzyme, is constituted by three subunits, I, II and III, conserved from prokaryotes to eukaryotes, encoded by the mitochondrial genome | 21320464 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
Q6QTG9_BOVIN,
A0A493ULV5_BOVIN
UniprotKB:
Q6QTG9,
A0A493ULV5
UniParc:
UPI000023FC35
EMBL:
AY526085
Ensembl:
ENSBTAG00000043561
KO:
bta:3283879
|
Nucleutide sequences |
EMBL-CDS:
AAS18244.1
Ensembl_TRS:
ENSBTAT00000060569
|
Protein sequencees |
Ensembl_PRO:
ENSBTAP00000053147
RefSeq:
YP_209207.1
|
Others |
UniRef100:
UniRef100_A0A493ULV5
UniRef90:
UniRef90_P00396
UniRef50:
UniRef50_P00395
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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