Substrate specificity and evolutionary implications of a NifDK enzyme carrying NifB-co at its active site.

Basem Soboh, Eric S Boyd, Dehua Zhao, John W Peters, Luis M Rubio

FEBS letters 2010 Apr 16

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The in vitro reconstitution of molybdenum nitrogenase was manipulated to generate a chimeric enzyme in which the active site iron-molybdenum cofactor (FeMo-co) is replaced by NifB-co. The NifDK/NifB-co enzyme was unable to reduce N(2) to NH(3), while exhibiting residual C(2)H(4) and considerable H(2) production activities. Production of H(2) by NifDK/NifB-co was stimulated by N(2) and was dependent on NifH and ATP hydrolysis. Thus, NifDK/NifB-co is a useful tool to gain insights into the catalytic mechanism of nitrogenase. Furthermore, phylogenetic analysis of D and K homologs indicates that several early emerging lineages, which contain NifB, NifH and NifDK encoding genes but which lack other genes required for processing NifB-co into FeMo-co, might encode an enzyme with similar catalytic properties to NifDK/NifB-co. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Basem Soboh, Eric S Boyd, Dehua Zhao, John W Peters, Luis M Rubio. Substrate specificity and evolutionary implications of a NifDK enzyme carrying NifB-co at its active site. FEBS letters. 2010 Apr 16;584(8):1487-92