Multiple Inequivalent Metal−Nucleotide Coordination Environments in the Presence of the VO2+-Inhibited Nitrogenase Iron Protein: pH-Dependent Structural Rearrangements at the Nucleotide Binding Site-Reference-Cited by-同舟云学术

Multiple Inequivalent Metal−Nucleotide Coordination Environments in the Presence of the VO2+-Inhibited Nitrogenase Iron Protein: pH-Dependent Structural Rearrangements at the Nucleotide Binding Site

Published:2002-10-11 Issue:44 Volume:41 Page:13253-13263
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Petersen Jan¹,Fisher Karl¹,Mitchell Claire J.¹,Lowe David J.¹

Affiliation:

1. Department of Biological Chemistry, John Innes Centre, Colney Lane, Norwich NR4 7UH, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0260029

Reference67 articles.

1. Mortenson, L. E., Seefeldt, L. C., Morgan, T. V., and Bolin, J. T. (1993) inAdvances in Enzymology(Meister, A., Ed.) Vol. 67, pp 299−374, Wiley & Sons, New York.

2. Mechanism of Molybdenum Nitrogenase

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