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- Sigfridsson, K.; Young, S.; Hansson, O.
- Biochemistry 1996 v.35 no.4 pp. 1249-1257
- histidine, etc ; Escherichia coli; absorption; alanine; asparagine; electron paramagnetic resonance spectroscopy; electron transfer; electrostatic interactions; glutamic acid; hydrophobicity; leucine; lysine; models; mutants; phenylalanine; photosystem I; plastocyanin; site-directed mutagenesis; spectral analysis; tyrosine; Show all 20 Subjects
- ... A series of plastocyanin mutants have been constructed by site-directed mutagenesis and expressed in Escherichia coli to elucidate the interaction between plastocyanin and photosystem 1 in the photosynthetic electron-transfer chain. Leu-12 has been replaced with alanine, asparagine, glutamate, and lysine, while Tyr-83 has been exchanged for histidine, phenylalanine, and leucine. Phe-35, Asp-42, an ...
- Chen, Y.L.; Park, S.; Thornburg, R.W.; Tabatabai, L.B.; Kintanar, A.
- Biochemistry 1995 v.34 no.38 pp. 12265-12275
- histidine, etc ; Brucella melitensis biovar Abortus; Escherichia coli; X-ray diffraction; active sites; amino acid sequences; cattle; copper; humans; metal ions; models; nitrogen; nuclear magnetic resonance spectroscopy; oxidation; prediction; protons; sequence alignment; superoxide dismutase; zinc; Show all 19 Subjects
- ... Prokaryotic Cu-Zn superoxide dismutases (SODs) are rare and poorly characterized compared to their eukaryotic counterparts. To better characterize the structure of the prokaryotic enzyme, an NMR investigation of Brucella abortus Cu-Zn SOD in the reduced form was undertaken. The enzyme studied was a recombinant form, expressed in Escherichia coli. The enzyme initially lacked a full complement of Cu ...