| First Author | Hüttemann M | Year | 2000 |
| Journal | Eur J Biochem | Volume | 267 |
| Issue | 7 | Pages | 2098-104 |
| PubMed ID | 10727950 | Mgi Jnum | J:61465 |
| Mgi Id | MGI:1355016 | Doi | 10.1046/j.1432-1327.2000.01216.x |
| Citation | Huttemann M, et al. (2000) Turkey cytochrome c oxidase contains subunit VIa of the liver type associated with low efficiency of energy transduction. Eur J Biochem 267(7):2098-104 |
| abstractText | Cytochrome c oxidase was isolated from turkey liver, heart and breast skeletal muscle and separated by SDS/PAGE. The N-terminal amino-acid sequence of subunit VIa from all tissues and internal sequences from the skeletal muscle enzyme show homology to the mammalian liver-type subunit VIaL, which was verified by isolation and sequencing of the cDNA of turkey subunit VIa. No cDNA corresponding to subunit VIaH (mammalian heart-type) could be found by RACE-PCR with mRNA from all turkey tissues. Measurement of proton translocation with the reconstituted enzymes from turkey liver and heart revealed H+/e- ratios below 0.5 that were independent of the intraliposomal ATP/ADP ratio, as previously found with the bovine liver enzyme. Under identical conditions, the bovine heart enzyme revealed H+/e- ratios of 0.85 at low and 0.48 at high intraliposomal ATP/ADP ratios. The results suggest that in birds the lower H+/e-ratio of cytochrome c oxidase participates in elevated resting metabolic rate and thermogenesis. |
