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J. Biochem, 1982, Vol. 91, No. 6 2077-2085
© 1982 Japanese Biochemical Society

research-article

Identity of the Heme-Not-Containing Protein in Bovine Heart Cytochrome c1 Preparation with the Protein Mediating c1-c Complex Formation—A Protein with High Glutamic Acid Content1

Sadao WAKABAYASHI*, Hideki TAKEDA*, Hiroshi MATSUBARA*, Chong H. KIM** and Tsoo E. KING**

*Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560
**Department of Chemistry and Laboratory of Bioenergetics, State University of New York Albany, New York 12222, U.S.A.

A heme-not-containing protein was isolated from cytochrome c1 preparation by gel filtration after carboxymethylation and citraconylation. The amino acid sequence of this protein was determined by the analyses of tryptic and chymotryptic peptides as well as by solid-phase sequence analysis. It consisted of 78 amino acid residues and the molecular weight was calculated to be 9,175. This protein contained a high proportion of glutamic acid and glutamine (27 % of the total residues) but no methionine, isoleucine, tyrosine, and tryptophan. The most notable feature was an acidic cluster of 8 consecutive glutamic acid residues near the amino(N)-terminus. The secondary structure was predicted to have a high proportion of helical content.

The amino acid composition and N-terminal sequence of a protein independently prepared from bovine heart mitochondria, which is essential to the formation of the cytochrome c1-c complex, suggested that this colorless factor and the present heme-not-containing protein are identical. Evidence shows that another protein, called the non-heme protein, isolated from "two-band" cytochrome c1 preparation is also the same protein as that presented in this paper.

1This work was supported in part by a Grant-in-Aid for Special Project Research (No. 56113004) to H. M. and grants from N1H (2 RO1 GM 16767 and NIH 5 RO1 HL 12576) and American Cancer Society (BC 349) to T.E.K.


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