Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase

Lin Ji, Manuel Becana, Gautam Sarath, Linda Shearman and Robert V. Klucas
Plant Physiology
Vol. 106, No. 1 (Sep., 1994), pp. 203-209
Stable URL: http://www.jstor.org/stable/4276042
Page Count: 7
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase
Preview not available

Abstract

We previously cloned and sequenced a cDNA encoding soybean ferric leghemoglobin reductase (FLbR), an enzyme postulated to play an important role in maintaining leghemoglobin in a functional ferrous state in nitrogen-fixing root nodules. This cDNA was sub-cloned into an expression plasmid, pTrcHis C, and overexpressed in Escherichia coli. The recombinant FLbR protein, which was purified by two steps of column chromatography, was catalytically active and fully functional. The recombinant FLbR cross-reacted with antisera raised against native FLbR purified from soybean root nodules. The recombinant FLbR, the native FLbR purified from soybean (Glycine max L.) root nodules, and dihydrolipoamide dehydrogenases from pig heart and yeast had similar but not identical ultraviolet-visible absorption and fluorescence spectra, cofactor binding, and kinetic properties. FLbR shared common structural features in the active site and prosthetic group binding sites with other pyridine nucleotide-disulfide oxidoreductases such as dihydrolipoamide dehydrogenases, but displayed different microenvironments for the prosthetic groups.

Page Thumbnails

  • Thumbnail: Page 
203
    203
  • Thumbnail: Page 
204
    204
  • Thumbnail: Page 
205
    205
  • Thumbnail: Page 
206
    206
  • Thumbnail: Page 
207
    207
  • Thumbnail: Page 
208
    208
  • Thumbnail: Page 
209
    209