ArticleThe Journal of biological chemistry2011
Spectroscopic studies on the [4Fe-4S] cluster in adenosine 5'-phosphosulfate reductase from Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Mössbauer spectroscopy in drug discovery: revealing Fe- and Fe-S cluster dependent targets.Expert opinion on drug discovery · 2026Review
- Distinct Valence States of the [4Fe4S] Cluster Revealed in the Hydrogenase CrHydA1.Angewandte Chemie (International ed. in English) · 2025Article
- A cytochrome cPlant communications · 2024Article
- The thiolation of uridine 34 in tRNA, which controls protein translation, depends on a [4Fe-4S] cluster in the archaeum Methanococcus maripaludis.Scientific reports · 2023Article
- Crystal Structure of the [4Fe-4S] Cluster-Containing Adenosine-5'-phosphosulfate Reductase fromACS omega · 2021Article
- Functional Site Discovery in a Sulfur Metabolism Enzyme by Using Directed Evolution.Chembiochem : a European journal of chemical biology · 2016Article
- Design, synthesis and evaluation of Fe-S targeted adenosine 5'-phosphosulfate reductase inhibitors.Nucleosides, nucleotides & nucleic acids · 2015Article
- A continuous spectrophotometric assay for adenosine 5'-phosphosulfate reductase activity with sulfite-selective probes.Analytical biochemistry · 2013Article
- New targets and inhibitors of mycobacterial sulfur metabolism.Infectious disorders drug targets · 2013Review
- Iron-sulfur cluster engineering provides insight into the evolution of substrate specificity among sulfonucleotide reductases.ACS chemical biology · 2012Article
- Deciphering the role of histidine 252 in mycobacterial adenosine 5'-phosphosulfate (APS) reductase catalysis.The Journal of biological chemistry · 2011Article
- Geometric and electrostatic study of the [4Fe-4S] cluster of adenosine-5'-phosphosulfate reductase from broken symmetry density functional calculations and extended X-ray absorption fine structure spectroscopy.Inorganic chemistry · 2011Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Mycobacterium tuberculosis adenosine 5'-phosphosulfate reductase (MtAPR) is an iron-sulfur protein and a validated target to develop new antitubercular agents, particularly for the treatment of latent infection. The enzyme harbors a [4Fe-4S](2+) cluster that is coordinated by four cysteinyl ligands, two of which are adjacent in the amino acid sequence. The iron-sulfur cluster is essential for catalysis; however, the precise role of the [4Fe-4S] cluster in APR remains unknown. Progress in this area has been hampered by the failure to generate a paramagnetic state of the [4Fe-4S] cluster that can be studied by electron paramagnetic resonance spectroscopy. Herein, we overcome this limitation and report the EPR spectra of MtAPR in the [4Fe-4S](+) state. The EPR signal is rhombic and consists of two overlapping S = ½ species. Substrate binding to MtAPR led to a marked increase in the intensity and resolution of the EPR signal and to minor shifts in principle g values that were not observed among a panel of substrate analogs, including adenosine 5'-diphosphate. Using site-directed mutagenesis, in conjunction with kinetic and EPR studies, we have also identified an essential role for the active site residue Lys-144, whose side chain interacts with both the iron-sulfur cluster and the sulfate group of adenosine 5'-phosphosulfate. The implications of these findings are discussed with respect to the role of the iron-sulfur cluster in the catalytic mechanism of APR.
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