ArticleBiochemistry2009
Characterization of [4Fe-4S]-containing and cluster-free forms of Streptomyces WhiD.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 75 citations in OpenAlex.
- Nitrite Causes Nitrosative Stress to Iron Sulfur Clusters.Journal of the American Chemical Society · 2025Article
- The Tumor Microbiome Reacts to Hypoxia and Can Influence Response to Radiation Treatment in Colorectal Cancer.Cancer research communications · 2024Article
- Structural basis of dual activation of cell division by the actinobacterial transcription factors WhiA and WhiB.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Elusive Mononitrosylated [FeAngewandte Chemie (International ed. in English) · 2022Article
- Mycobacterium tuberculosis whiB3 and Lipid Metabolism Genes Are Regulated by Host Induced Oxidative StressMicroorganisms · 2022Article
- WblA, a global regulator of antibiotic biosynthesis in Streptomyces.Journal of industrial microbiology & biotechnology · 2021Review
- SufR, a [4Fe-4S] Cluster-Containing Transcription Factor, Represses theApplied and environmental microbiology · 2020Article
- Interaction of theThe Journal of biological chemistry · 2020Article
- The FeoC [4Fe-4S] Cluster Is Redox-Active and Rapidly Oxygen-Sensitive.Biochemistry · 2019Article
- A Novel Two-Component System, Encoded by the sFrontiers in microbiology · 2019Article
- The actinobacterial WhiB-like (Wbl) family of transcription factors.Molecular microbiology · 2018Review
- wblE2 transcription factor in Streptomyces griseus S4-7 plays an important role in plant protection.MicrobiologyOpen · 2017Article
- Article
- Nitrosylation of Nitric-Oxide-Sensing Regulatory Proteins Containing [4Fe-4S] Clusters Gives Rise to Multiple Iron-Nitrosyl Complexes.Angewandte Chemie (International ed. in English) · 2016Article
- Engineering a functional 1-deoxy-D-xylulose 5-phosphate (DXP) pathway in Saccharomyces cerevisiae.Metabolic engineering · 2016Article
- Iron-sulfur cluster exchange reactions mediated by the human Nfu protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Article
- Biochemical properties of Paracoccus denitrificans FnrP: reactions with molecular oxygen and nitric oxide.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- PqqE from Methylobacterium extorquens AM1: a radical S-adenosyl-l-methionine enzyme with an unusual tolerance to oxygen.Journal of biochemistry · 2016Article
- c-di-GMP signalling and the regulation of developmental transitions in streptomycetes.Nature reviews. Microbiology · 2015Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
WhiD, a member of the WhiB-like (Wbl) family of iron-sulfur proteins found exclusively within the actinomycetes, is required for the late stages of sporulation in Streptomyces coelicolor. Like all other Wbl proteins, WhiD has not so far been purified in a soluble form that contains a significant amount of cluster, and characterization has relied on cluster-reconstituted protein. Thus, a major goal in Wbl research is to obtain and characterize native protein containing iron-sulfur clusters. Here we report the analysis of S. coelicolor WhiD purified anaerobically from Escherichia coli as a soluble protein containing a single [4Fe-4S](2+) cluster ligated by four cysteines. Upon exposure to oxygen, spectral features associated with the [4Fe-4S] cluster were lost in a slow reaction that unusually yielded apo-WhiD directly without significant concentrations of cluster intermediates. This process was found to be highly pH dependent with an optimal stability observed between pH 7.0 and pH 8.0. Low molecular weight thiols, including a mycothiol analogue and thioredoxin, exerted a small but significant protective effect against WhiD cluster loss, an activity that could be of physiological importance. [4Fe-4S](2+) WhiD was found to react much more rapidly with superoxide than with either oxygen or hydrogen peroxide, which may also be of physiological significance. Loss of the [4Fe-4S] cluster to form apoprotein destabilized the protein fold significantly but did not lead to complete unfolding. Finally, apo-WhiD exhibited negligible activity in an insulin-based disulfide reductase assay, demonstrating that it does not function as a general protein disulfide reductase.
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