ArticleeLife2015
Structural basis of interprotein electron transfer in bacterial sulfite oxidation.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Analysis of microbial community evolution, autolysis phenomena, and energy metabolism pathways inFrontiers in microbiology · 2024Article
- A novel bacterial sulfite dehydrogenase that requires threeApplied and environmental microbiology · 2023Article
- The structure of the complex between the arsenite oxidase from Pseudorhizobium banfieldiae sp. strain NT-26 and its native electron acceptor cytochrome cActa crystallographica. Section D, Structural biology · 2023Article
- Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins.Inorganic chemistry · 2022Article
- Generation and Physiology of Hydrogen Sulfide and Reactive Sulfur Species in Bacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Deconvolution of reduction potentials of formate dehydrogenase from Cupriavidus necator.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Control of Bacterial Sulfite Detoxification by Conserved and Species-Specific Regulatory Circuits.Frontiers in microbiology · 2019Article
- MostmSphere · 2018Article
- Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode.The EMBO journal · 2017Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE SorT from Sinorhizobium meliloti and its cognate electron acceptor SorU. Kinetic and thermodynamic analyses of the SorT/SorU interaction show the complex is dynamic in solution, and that the proteins interact with Kd = 13.5 ± 0.8 μM. The crystal structures of the oxidized SorT and SorU, both in isolation and in complex, reveal the interface to be remarkably electrostatic, with an unusually large number of direct hydrogen bonding interactions. The assembly of the complex is accompanied by an adjustment in the structure of SorU, and conformational sampling provides a mechanism for dissociation of the SorT/SorU assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.