Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

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.


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

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 20219465

View Full Text