Functional Characterization of Fdx1: Evidence for an Evolutionary Relationship between P450-Type and ISC-Type Ferredoxins
| Autor: | Rita Bernhardt, Stefania Iametti, Kerstin Maria Ewen, Anna Morleo, Frank Hannemann |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Iron-Sulfur Proteins
inorganic chemicals Iron Molecular Sequence Data Sulfite Reductase (Ferredoxin) Evolution Molecular chemistry.chemical_compound Bacterial Proteins Biosynthesis Structural Biology Adrenodoxin Animals Amino Acid Sequence Cholesterol Side-Chain Cleavage Enzyme Myxococcales Cloning Molecular Molecular Biology Phylogeny Ferredoxin Sorangium cellulosum Aconitate Hydratase Sequence Homology Amino Acid biology Phylogenetic tree Circular Dichroism Computational Biology Cytochrome P450 biology.organism_classification Mitochondria Biochemistry chemistry biology.protein Ferredoxins Cattle ISCU Oxidation-Reduction NADP Function (biology) |
| Zdroj: | Journal of Molecular Biology. 413:940-951 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2011.09.010 |
| Popis: | Ferredoxins are ubiquitous proteins with electron transfer activity involved in a variety of biological processes. In this work, we investigated the characteristics and function of Fdx1 from Sorangium cellulosum So ce56 by using a combination of bioinformatics and of biochemical/biophysical approaches. We were able to experimentally confirm a role of Fdx1 in the iron–sulfur cluster biosynthesis by in vitro reduction studies with cluster-loaded So ce56 IscU and by transfer studies of the cluster from the latter protein to apo-aconitase A. Moreover, we found that Fdx1 can replace mammalian adrenodoxin in supporting the activity of bovine CYP11A1. This makes S. cellulosum Fdx1 the first prokaryotic ferredoxin reported to functionally interact with this mammalian enzyme. Although the interaction with CYP11A1 is non-physiological, this is—to the best of our knowledge—the first study to experimentally prove the activity of a postulated ISC-type ferredoxin in both the ISC assembly and a cytochrome P450 system. This proves that a single ferredoxin can be structurally able to provide electrons to both cytochromes P450 and IscU and thus support different biochemical processes. Combining this finding with phylogenetic and evolutionary trace analyses led us to propose the evolution of eukaryotic mitochondrial P450-type ferredoxins and ISC-type ferredoxins from a common prokaryotic ISC-type ancestor. |
| Databáze: | OpenAIRE |
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