Nature of Oxygen Inhibition of Nitrogenase from Azotobacter vinelandii | Zendy

Peter P. Wong | Zendy; R. H. Burris | Zendy

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Nature of Oxygen Inhibition of Nitrogenase from Azotobacter vinelandii

Author(s) -

Peter P. Wong,

R. H. Burris

Publication year - 1972

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.69.3.672

Subject(s) - azotobacter vinelandii , nitrogenase , azotobacter , oxygen , cyanide , azide , chemistry , acetylene , photochemistry , dcmu , nitrogen fixation , substrate (aquarium) , nitrogen , biochemistry , inorganic chemistry , photosystem ii , organic chemistry , bacteria , photosynthesis , biology , ecology , genetics

The reduction of nitrogen, acetylene, azide, and cyanide at various oxygen concentrations by nitrogenase from Azotobacter vinelandii was measured with a well-defined system. Oxygen inhibited the reduction of each substrate uncompetitively. The inhibition constants (K(i)) were 0.014, 0.023, 0.008, and 0.003 atm of oxygen for reduction of nitrogen, acetylene, azide, and cyanide, respectively. The system used included ATP-generating components, subcellular particles from A. vinelandii with high nitrogenase specific activity, and illuminated spinach chloroplasts plus carriers to supply electrons. Oxygen did not affect the photochemical electron donating system, but it did inhibit nitrogenase-dependent ATP hydrolysis.

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