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Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria
Author(s) -
Runswick Michael J.,
Fearnley Ian M.,
Skehel J.Mark,
Walker John E.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80955-3
Subject(s) - biochemistry , acyl carrier protein , oxidoreductase , serine , chemistry , peptide sequence , molecular mass , protein subunit , enzyme , biology , biosynthesis , gene
The amino‐acid sequence of a subunit of NADH:ubiquinone oxidoreductase from bovine heart mitochondria has been determined and is closely related to those of acyl carrier proteins that are involved in fatty acid biosynthesis in Escherichia coli and plants. Evidence for the presence of covalently attached pantetheine‐4′‐phosphate in the bovine protein has been obtained by determination of the molecular mass of the isolated subunit by electrospray mass spectrometry, before and after incubation of the protein at alkaline pH under reducing conditions. This decreased the molecular mass from 10751.6 to 10449.4, a difference of 302.2 mass units; the value calculated from the protein sequence with one covalently attached pantetheine‐4′‐phosphate is 10449.8. The acyl group which is removed by alkaline reduction, appears to be attached via a thioester linkage, By analogy with the bacterial protein it is likely that the attachment site of the pantetheine‐4‐phosphate is serine‐44, which is found in a highly conserved region of the sequence. At present the function of the acyl carrier protein in mitochondrial complex I is not understood.