Reduction of nitrogenase Fe protein from Azotobacter vinelandii by dithionite: quantitative and qualitative effects of nucleotides, temperature, pH and reaction buffer-Reference-Cited by-同舟云学术

Reduction of nitrogenase Fe protein from Azotobacter vinelandii by dithionite: quantitative and qualitative effects of nucleotides, temperature, pH and reaction buffer

Published:2004-05 Issue:2 Volume:109 Page:305-324
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Wilson P.E.,Bunker J.,Lowery T.J.,Watt G.D.

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference29 articles.

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2. Nitrogenase of Azotobacter chroococcum kinetics of the reduction of oxidized iron protein by sodium dithionite;Thorneley;Biochem. J.,1976

3. Nitrogenase of Klebsiella pneumoniae. Kinetic studies on the iron protein involving reduction by sodium dithionite, the binding of magnesium ADP and a conformation change that alters the reactivity of the iron–sulfur (4Fe–4S) center;Ashby;Biochem. J.,1987

4. The Vanadium-and Molybdenum-containing nitrogenases of Azotobacter chroococcum. Comparison of mid-point potentials and kinetics of reduction by sodium dithionite of the iron proteins with bound magnesium adenosine 5′-Diphosphate;Bergstrom;Biochem. J.,1988

5. Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: Characterization of a tight protein–protein complex;Lanzilotta;Biochemistry,1996

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