Bui, P. T. and Mortenson, L. E. (1968) Mechanism of the Enzymic Reduction of N_2: The Binding of Adenosine 5'-Triphosphate and Cyanide to the N_2-reducing System. Proceedings of the National Academy of Sciences of the United States of America, 61 (3). pp. 1021-1027. ISSN 0027-8424. PMCID PMC305430. http://resolver.caltech.edu/CaltechAUTHORS:BUIpnas68
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The in vitro reduction of N_2 is a complex process involving at least six different reactants: two proteins [1,2] for which the names azoferredoxin (AzoFd) and molybdoferredoxin (MoFd) have been proposed, an electron source, the electron acceptor, ATP, and Mg2+[5-7]. One of the goals of research in this area is to define the orderly and quantitative participation of these reactants leading to the reduction of the electron acceptor with concomitant breakdown of ATP to ADP and inorganic phosphate. The work described in this paper shows that (1) AzoFd reversibly binds both ATP, a reactant in N2 reduction, and ADP, a specific inhibitor of N2 reduction, and (2) MoFd reversibly binds cyanide, which is also reduced by the N_2-reducing system. It is suggested that the binding of ATP and of cyanide are partial reactions of the N_2-reducing system.
|Additional Information:||© 1968 National Academy of Sciences. Communicated by Martin D. Kamen, August 27, 1968. We appreciate the capable preparative skills of Mrs. Dorothy Sheets and Mrs. Claudette Polis. We thank Professor W. J. Ray, Jr., for generous advice. Supported by NIH grant AI04865-06.|
|PubMed Central ID:||PMC305430|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Archive Administrator|
|Deposited On:||18 Sep 2006|
|Last Modified:||27 Mar 2017 15:47|
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