Nonheme Iron Proteins. IV. Structural Studies of Micrococcus aerogenes Rubredoxin

H. Bachmayer, A. M. Benson, K. T. Yasunobu, W. T. Garrard, H. R. Whiteley

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Abstract

The S-β-aminoethylcysteinyl derivative of Micrococcus aerogenes rubredoxin was digested with trypsin and chymotrypsin in separate experiments. The fragments were purified and their sequences were determined by standard procedures. From the sequences of the individual peptides and the overlaps between them, the total amino acid sequence of the M. aerogenes rubredoxin was deduced. The stability of the chelate structure of this protein in dilute acids, 8 M urea, 50% ethanol, and 2.5 and 5 M guanidine hydrochloride was determined with respect to time. These studies and the resistance of the native protein to proteolytic digestion suggest a compact and stable confirmation for the native protein.

Original languageEnglish (US)
Pages (from-to)986-996
Number of pages11
JournalBiochemistry
Volume7
Issue number3
DOIs
StatePublished - Mar 1 1968

ASJC Scopus subject areas

  • Biochemistry

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    Bachmayer, H., Benson, A. M., Yasunobu, K. T., Garrard, W. T., & Whiteley, H. R. (1968). Nonheme Iron Proteins. IV. Structural Studies of Micrococcus aerogenes Rubredoxin. Biochemistry, 7(3), 986-996. https://doi.org/10.1021/bi00843a016