Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1. J Biol Inorg Chem 2002 Apr;7(4-5):526-32
Date
04/10/2002Pubmed ID
11941510DOI
10.1007/s00775-001-0330-2Scopus ID
2-s2.0-0036934396 (requires institutional sign-in at Scopus site) 69 CitationsAbstract
Eukaryotic Isa1 is one of several mitochondrial proteins that have been implicated in Fe-S cluster assembly paths in vivo. We report the first biochemical characterization of an eukaryotic member of this family and discuss this in the context of results from in vivo studies and studies of bacterial homologues. Schizosaccharomyces pombe Isa1 is a multimeric protein carrying [2Fe-2S](2+) clusters that have been characterized by Mössbauer and optical spectroscopic studies. Complex formation with a redox-active ferredoxin has been identified through crosslinking experiments and the coordination chemistry and stability of the native clusters has been investigated through site-directed mutagenesis and spectroscopic analysis. Electronic supplementary material to this paper, containing Mössbauer and UV-visible spectra for mutant Isa1 proteins, can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0330-2.
Author List
Wu G, Mansy SS, Hemann C, Hille R, Surerus KK, Cowan JAAuthor
Kristene K. Surerus in the Chemistry and Biochemistry department at University of Wisconsin - MilwaukeeMESH terms used to index this publication - Major topics in bold
AlanineAmino Acid Sequence
Cloning, Molecular
Cross-Linking Reagents
Cysteine
DNA-Binding Proteins
Electron Spin Resonance Spectroscopy
Escherichia coli
Ferredoxins
Iron-Sulfur Proteins
Molecular Sequence Data
Mutation
Saccharomyces cerevisiae Proteins
Schizosaccharomyces
Sequence Homology, Amino Acid
Spectroscopy, Mossbauer
Transcription Factors
