Comparison of active and inactive forms of iron protein from Rhodospirillum rubrum.
The Fe protein of nitrogenase from Rhodospirillum rubrum was purified in its active and inactive forms. It is shown that the inactive form exists as a two-subunit modified form of the enzyme as previously reported [Ludden & Burris (1978) Biochem. J. 175, 251--259]. In contrast, the active form exists as a single-subunit unmodified form of the enzyme. The upper subunit (on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis) of the inactive form was shown to contain at least the phosphate group of the covalently bound modifying group. The active and inactive forms of the enzyme were shown to be identical proteins on the basis of amino-acid composition, tryptic-digest pattern and immunological cross-reactivity.
D000596:Amino Acids / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007527:Isoenzymes / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D009591:Nitrogenase / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D010088:Oxidoreductases; D010446:Peptide Fragments / Q000032:analysis; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D013053:Spectrophotometry
D000596:Amino Acids; D007527:Isoenzymes; D010446:Peptide Fragments; D010088:Oxidoreductases; D009591:Nitrogenase; C029130:nitrogenase reductase