Thiol reactivity of the nitrogenase Fe-protein from Azotobacter vinelandii.
1983; Elsevier BV; Volume: 258; Issue: 22 Linguagem: Inglês
10.1016/s0021-9258(17)43939-1
ISSN1083-351X
AutoresRobert P. Hausinger, James B. Howard,
Tópico(s)Metal-Catalyzed Oxygenation Mechanisms
ResumoA procedure has been developed to examine some of the functional roles of the14 cysteinyl residues in the nitrogenase Fe-protein (Av2) from Azotobacter vinelandii.The reduced form of Av2 was alkylated with iod0[2-'~C]acetic acid under a variety of experimental conditions, e.g.reaction in the presence of nucleotides, a,a'-dipyridyl and nucleotides, or denaturants.The labeled cysteinyl residues were identified and quantified using an analytical DEAE-Sepharose ion exchange chromatography peptide mapping technique based upon the known amino acid sequence (Hausinger, R.
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