Abstract
An answer was sought to the question: “Why is the Fe protein inactive as purified from Rhodospirillum rubrum grown on glutamate as its nitrogen source?”. The inactive Fe protein proved capable of binding MgATP and undergoing a conformation shift upon binding MgATP. The protein could be reversibly oxidized and reduced, but it was incapable of transferring electrons to MoFe protein at a substantial rate. Because of this impaired ability of inactive Fe protein to transfer electrons to MoFe protein, the nitrogenase complex of active MoFe protein and inactive Fe protein is incapable of hydrolyzing MgATP or of reducing acetylene or N 2 at substantial rates.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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