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Escherichia coli formate dehydrogenase mutants with altered selenopolymer profiles

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Abstract

Four classes of Escherichia coli mutants deficient in either or both of their anaerobic selenium-containing formate dehydrogenases (FDH) were isolated. A class I mutant devoid of FDHH activity specifically linked to benzyl viologen (BV) produced a small amount of the FDHH 80,000 dalton selenopeptide. Three class II mutants were deficient in FDHN activity specifically linked to phenazine methosulfate (PMS) and exhibited a selenopeptide “doublet” rather than the FDHN 110,000 dalton selenosubunit. Three class III mutants were selenium incorporation deficient and did not exhibit either FDH activity or 75Selabeled selenopolymers. A class IV mutant was devoid of PMS-linked FDHN activity; neither its FDHN 110,000 dalton selenosubunit nor its BV-linked FDHH activity was fully regulated by nitrate.

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Abbreviations

FDH:

formate dehydrogenase

BV:

benzyl viologen

MV:

methyl viologen

PMS:

phenazine methosulfate

SDS-PAGE:

sodium dodecyl sulfate-polyacrylamide gel electrophoresis

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Author notes

  1. J. C. Cox

    Present address: Research and Development, Applied Poly Technology, Inc., 8030 El Rio, 77054, Houston, TX, USA

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Texas, Medical School, 77025, Houston, TX, USA

    J. C. Cox

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  1. J. C. Cox
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Cox, J.C. Escherichia coli formate dehydrogenase mutants with altered selenopolymer profiles. Arch. Microbiol. 152, 397–400 (1989). https://doi.org/10.1007/BF00425180

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  • DOI: https://doi.org/10.1007/BF00425180

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