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Mechanism of the Enzymic Reduction of N2: The Binding of Adenosine 5'-Triphosphate and Cyanide to the N2-reducing System

Bui, P. T. and Mortenson, L. E. (1968) Mechanism of the Enzymic Reduction of N2: The Binding of Adenosine 5'-Triphosphate and Cyanide to the N2-reducing System. Proceedings of the National Academy of Sciences of the United States of America, 61 (3). pp. 1021-1027. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:BUIpnas68

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Abstract

The in vitro reduction of N2 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[3], an electron source, the electron acceptor, ATP[4], 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[7]. 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 N2-reducing system. It is suggested that the binding of ATP and of cyanide are partial reactions of the N2-reducing system.


Item Type:Article
Additional Information:Copyright © 1968 by the 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.
Record Number:CaltechAUTHORS:BUIpnas68
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:BUIpnas68
Alternative URL:http://www.pnas.org/content/vol61/issue3/
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ID Code:5001
Collection:CaltechAUTHORS
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Deposited On:18 Sep 2006
Last Modified:26 Dec 2012 09:03

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