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Title: Amino-terminal sequences of the L,M, and H subunits of reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00259a019· OSTI ID:6123793
 [1]; ; ;
  1. Massachusetts Inst. of Tech., Cambridge

We have determined the sequence of the 25-28 amino-terminal residues of the three subunits, L,M, and H, of the membrane-bound reaction center protein of the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26. The sequences are as follows: L, H/sub 2/N-Ala-Leu-Leu-Ser-Phe-Glu-Arg-Lys-Tyr-Arg-Val-Pro-Gly-Gly-Thr-Leu-Val-Gly-Gly-Asn-Leu-Phe-Asp-Phe-(His)-Val-; M, H/sub 2/N-Ala-Glu-Tyr-Gln-Asn-Ile-Phe-Ser-Gln-Val-Gln-Val-Arg-Gly-Pro-Ala-Asp-Leu-Gly-Met-Thr-Glu-Asp-Val-Asn-Leu-Ala-Asn-; H, H/sub 2/N-Met-Val-Gly-Val-Thr-Ala-Phe-Gly-Asn-Phe-Asp-Leu-Ala-Ser-Leu-Ala-Ile-Tyr-Ser-Phe-Trp-Ile-Phe-Leu-Ala-X-Leu-Ile-. The H sequence, especially after the aspartyl residue at position 11, is rich in hydrophobic residues, consistent with the possibility that this section of the polypeptide chain is located within the membrane. The L sequence is hydrophilic near the amino terminus and then becomes moderately hydrophobic. The M sequence is of average polarity.

OSTI ID:
6123793
Journal Information:
Biochemistry; (United States), Vol. 21
Country of Publication:
United States
Language:
English