volume 32, issue 40, P10885-10893 1993
DOI: 10.1021/bi00091a044
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J. W. Farchaus, J. Wachtveitl, P. Mathis, D. Oesterhelt

Abstract: Five site-directed mutants were engineered to substitute phenylalanine, serine, leucine, methionine, and glycine for tyrosine residue 162 of the pufL gene in Rhodobacter (R.) sphaeroides. Each of the mutations and the wild-type (WT) genes was expressed in the R. sphaeroides puf deletion strain PUF delta LMX21/3. Initial characterization revealed that all of the mutants were photoheterotrophically competent but that L162G and L162S were impaired. The amounts of mutant reaction centers expressed, the spectral ch…

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