Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 281, Issue 43, Pages 32724-32727Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M607135200
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Funding
- Medical Research Council [MC_U105663141, MC_U105663148] Funding Source: Medline
- Medical Research Council [MC_U105663148, MC_U105663141] Funding Source: researchfish
- MRC [MC_U105663141, MC_U105663148] Funding Source: UKRI
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Mammalian mitochondrial complex I is a multisubunit membrane-bound assembly with a molecular mass approaching 1 MDa. By comprehensive analyses of the bovine complex and its constituent subcomplexes, 45 different subunits have been characterized previously. The presence of a 46th subunit was suspected from the consistent detection of a molecular mass of 10,566 by electrospray ionization mass spectrometry of subunits fractionated by reverse-phase high pressure liquid chromatography. The component was found associated with both the intact complex and subcomplex I beta, which represents most of the membrane arm of the complex, and it could not be resolved chromatographically from subunit SGDH( the subunit of bovine complex I with the N-terminal sequence Ser-Gly-Asp-His). It has now been characterized by tandem mass spectrometry of intact protein ions and shown to be a C-terminal fragment of subunit SGDH arising from a specific peptide bond cleavage between Ile-55 and Pro-56 during the electrospray ionization process. Thus, the subunit composition of bovine complex I has been established. It is a complex of 45 different proteins plus non-covalently bound FMN and eight iron-sulfur clusters.
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