Ontology highlight
ABSTRACT:
SUBMITTER: Wachnowsky C
PROVIDER: S-EPMC5167677 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
Wachnowsky Christine C Fidai Insiya I Cowan J A JA
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 20160818 7
Human Nfu is an iron-sulfur cluster protein that has recently been implicated in multiple mitochondrial dysfunctional syndrome (MMDS1). The Nfu family of proteins shares a highly homologous domain that contains a conserved active site consisting of a CXXC motif. There is less functional conservation between bacterial and human Nfu proteins, particularly concerning their Iron-sulfur cluster binding and transfer roles. Herein, we characterize the cluster exchange chemistry of human Nfu and its cap ...[more]