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ApoNifH functions in iron–molybdenum cofactor synthesis and apodinitrogenase maturation

By Priya Rangaraj, Vinod K. Shah and Paul W. Ludden

Abstract

NifH (dinitrogenase reductase) has three important roles in the nitrogenase enzyme system. In addition to its role as the obligate electron donor to dinitrogenase, NifH is required for the iron–molybdenum cofactor (FeMo-co) synthesis and apodinitrogenase maturation. We have investigated the requirement of the Fe–S cluster of NifH for these processes by preparing apoNifH. The 4Fe–4S cluster of NifH was removed by chelation of the cluster with α, α′-bipyridyl. The resulting apoNifH was tested in in vitro FeMo-co synthesis and apodinitrogenase maturation reactions and was found to function in both these processes. Thus, the presence of a redox active 4Fe–4S cluster in NifH is not required for its function in FeMo-co synthesis and in apodinitrogenase maturation. This, in turn, implies that the role of NifH in these processes is not one of electron transfer or of iron or sulfur donation

Topics: Biological Sciences
Publisher: The National Academy of Sciences of the USA
Year: 1997
OAI identifier: oai:pubmedcentral.nih.gov:23431
Provided by: PubMed Central
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