ArticleThe Journal of biological chemistry2010
Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Protein protein Interactions of NarL with NarG, SsrB, and FNR Proteins in Salmonella Typhimurium: A Comparative Analysis.Current microbiology · 2025Article
- Stabilization of the catalytically active structure of a molybdenum-dependent formate dehydrogenase depends on a highly conserved lysine residue.The FEBS journal · 2025Article
- GCompip: a pipeline for estimating the gene abundance in microbial communities.Bioinformatics advances · 2025Article
- Evolution and Competitive Struggles ofInternational journal of molecular sciences · 2024Article
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Robust Production, Crystallization, Structure Determination, and Analysis of [Fe-S] Proteins: Uncovering Control of Electron Shuttling and Gating in the Respiratory Metabolism of Molybdopterin Guanine Dinucleotide Enzymes.Methods in enzymology · 2018Article
- Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism.Scientific reports · 2016Article
- Perchlorate Reductase Is Distinguished by Active Site Aromatic Gate Residues.The Journal of biological chemistry · 2016Article
- Determining Roles of Accessory Genes in Denitrification by Mutant Fitness Analyses.Applied and environmental microbiology · 2016Article
- Structural and mechanistic insights on nitrate reductases.Protein science : a publication of the Protein Society · 2015Review
- Pyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate Reductase.The Journal of biological chemistry · 2015Article
- Phylogenomics of Mycobacterium Nitrate Reductase Operon.Current microbiology · 2015Review
- Dynamic subcellular localization of a respiratory complex controls bacterial respiration.eLife · 2015Article
- Emerging critical roles of Fe-S clusters in DNA replication and repair.Biochimica et biophysica acta · 2015Review
- The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.Biochimica et biophysica acta · 2015Review
- Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- Biosynthesis and Insertion of the Molybdenum Cofactor.EcoSal Plus · 2015Review
- Q-site occupancy defines heme heterogeneity in Escherichia coli nitrate reductase A (NarGHI).Biochemistry · 2014Article
- Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion.The Journal of biological chemistry · 2011Article
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6 authors.
Funding
Abstract
We have used site-directed mutagenesis, EPR spectroscopy, redox potentiometry, and protein crystallography to monitor assembly of the FS0 [4Fe-4S] cluster and molybdo-bis(pyranopterin guanine dinucleotide) cofactor (Mo-bisPGD) of the Escherichia coli nitrate reductase A (NarGHI) catalytic subunit (NarG). Cys and Ser mutants of NarG-His(49) both lack catalytic activity, with only the former assembling FS0 and Mo-bisPGD. Importantly, both prosthetic groups are absent in the NarG-H49S mutant. EPR spectroscopy of the Cys mutant reveals that the E(m) value of the FS0 cluster is decreased by at least 500 mV, preventing its participation in electron transfer to the Mo-bisPGD cofactor. To demonstrate that decreasing the FS0 cluster E(m) results in decreased enzyme activity, we mutated a critical Arg residue (NarG-Arg(94)) in the vicinity of FS0 to a Ser residue. In this case, the E(m) of FS0 is decreased by 115 mV, with a concomitant decrease in enzyme turnover to approximately 30% of the wild type. Analysis of the structure of the NarG-H49S mutant reveals two important aspects of NarGHI maturation: (i) apomolybdo-NarGHI is able to bind GDP moieties at their respective P and Q sites in the absence of the Mo-bisPGD cofactor, and (ii) a critical segment of residues in NarG, (49)HGVNCTG(55), must be correctly positioned to ensure holoenzyme maturation.
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