ArticleBiochemical and biophysical research communications2020
Heme inhibits the activity of a c-di-GMP phosphodiesterase in Vibrio cholerae.
Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Roles of divalent metals in the regulation of cyclic di-GMP signaling in bacteria.Journal of bacteriology · 2026Review
- Article
- Negative regulation of biofilm formation by nitric oxide sensing proteins.Biochemical Society transactions · 2023Review
- NosP Detection of Heme ModulatesBiochemistry · 2023Article
- Sensory Perception in Bacterial Cyclic Diguanylate Signal Transduction.Journal of bacteriology · 2022Review
- Nitric oxide stimulates type IV MSHA pilus retraction inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Recent evidence for multifactorial biofilm regulation by heme sensor proteins NosP and H-NOX.Chemistry letters · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Heme, a complex of iron and protoporphyrin IX, plays an essential role in numerous biological processes including oxygen transport, oxygen storage, and electron transfer. The role of heme as a prosthetic group in bacterial hemoprotein gas sensors, which utilize heme as a cofactor for the binding of diatomic gas molecules, has been well studied. Less well known is the role of protein sensors of heme. In this report, we characterize the heme binding properties of a phosphodiesterase, CdpA, from Vibrio cholerae. We demonstrate that the N-terminal domain of CdpA is a NosP domain capable of heme binding, which consequently inhibits the c-di-GMP hydrolysis activity of the C-terminal phosphodiesterase domain. Further evidence for CdpA as a heme responsive sensor is supported by a relatively fast rate of heme dissociation. This study provides insight into an emerging class of heme-responsive sensor proteins.
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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.