| First Author | Duborjal H | Year | 1997 |
| Journal | FEBS Lett | Volume | 405 |
| Issue | 3 | Pages | 345-50 |
| PubMed ID | 9108316 | Mgi Jnum | J:39849 |
| Mgi Id | MGI:87198 | Doi | 10.1016/s0014-5793(97)00212-3 |
| Citation | Duborjal H, et al. (1997) Immuno-purification of a dimeric subcomplex of the respiratory NADH-CoQ reductase of Rhodobacter capsulatus equivalent to the FP fraction of the mitochondrial complex I. FEBS Lett 405(3):345-50 |
| abstractText | The Rhodobacter capsulatus genes encoding the NUOE and NUOF subunits, equivalent to the 24 kDa and 51 kDa subunits of the mammalian mitochondrial complex I, have been sequenced. According to the nucleotide sequence, the NUOE subunit is 389 amino acids long and has a molecular mass of 41.3 kDa. In comparison to the mitochondrial equivalent subunit, NUOE is extended at the C terminus by more than 150 amino acids. The NUOF subunit is 431 amino acids long and has a molecular mass of 47.1 kDa. A subcomplex containing both the NUOE and NUOF subunits was extracted by detergent treatment of R. capsulatus membranes and immuno-purified. This subcomplex is homologous to the mitochondrial FP fragment. Mass spectrometry after trypsin treatment of the NUOE subunit validates the atypical primary structure deduced from the sequence of the gene. |
