ArticleProtein science : a publication of the Protein Society2018
Structure, function and evolution of the hemerythrin-like domain superfamily.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 56 citations in OpenAlex.
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- In vivo visualization of bioactive iron and oxygen using LiON, the labile iron and oxygen notifier.Cell reports methods · 2026Article
- Identification of a novel gene inAntimicrobial agents and chemotherapy · 2026Article
- Diverse bacteriohemerythrin genes ofmBio · 2025Article
- Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins.Nature communications · 2025Article
- The NmpRSTU multi-component signaling system ofJournal of bacteriology · 2025Article
- Proteomic evidence for aerobic methane production in groundwater by methylotrophic Methylotenera.The ISME journal · 2025Article
- Expression of hemerythrin-like genes from the obligate aerobeFrontiers in microbiology · 2025Article
- Transcriptomic characterization of recombinantApplied and environmental microbiology · 2024Article
- Nitrogen fixation in the widely distributed marine γ-proteobacterial diazotrophScience advances · 2024Article
- Single-cell RNA-seq reveals distinct metabolic "microniches" and close host-symbiont interactions in deep-sea chemosynthetic tubeworm.Science advances · 2024Article
- ConservedBiochemistry · 2024Article
- Transcriptomic profiling of haloarchaeal denitrification through RNA-Seq analysis.Applied and environmental microbiology · 2024Article
- The anti-amoebic activity of Pinus densiflora leaf extract against the brain-eating amoeba Naegleria fowleri.Parasites, hosts and diseases · 2024Article
- Comparative genomics of the niche-specific plant pathogenApplied and environmental microbiology · 2023Article
- The transcriptomic landscape of Magnetospirillum gryphiswaldense during magnetosome biomineralization.BMC genomics · 2022Article
- Repair of Iron Center Proteins-A Different Class of Hemerythrin-like Proteins.Molecules (Basel, Switzerland) · 2022Review
- Encapsulins.Annual review of biochemistry · 2022Review
- The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress.Journal of the American Chemical Society · 2022Article
- Structural and electronic properties of the active site of [ZnFe] SulE.Frontiers in molecular biosciences · 2022Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemerythrin-like proteins have generally been studied for their ability to reversibly bind oxygen through their binuclear nonheme iron centers. However, in recent years, it has become increasingly evident that some members of the hemerythrin-like superfamily also participate in many other biological processes. For instance, the binuclear nonheme iron site of YtfE, a hemerythrin-like protein involved in the repair of iron centers in Escherichia coli, catalyzes the reduction of nitric oxide to nitrous oxide, and the human F-box/LRR-repeat protein 5, which contains a hemerythrin-like domain, is involved in intracellular iron homeostasis. Furthermore, structural data on hemerythrin-like domains from two proteins of unknown function, PF0695 from Pyrococcus furiosus and NMB1532 from Neisseria meningitidis, show that the cation-binding sites, typical of hemerythrin, can be absent or be occupied by metal ions other than iron. To systematically investigate this functional and structural diversity of the hemerythrin-like superfamily, we have collected hemerythrin-like sequences from a database comprising fully sequenced proteomes and generated a cluster map based on their all-against-all pairwise sequence similarity. Our results show that the hemerythrin-like superfamily comprises a large number of protein families which can be classified into three broad groups on the basis of their cation-coordinating residues: (a) signal-transduction and oxygen-carrier hemerythrins (H-HxxxE-HxxxH-HxxxxD); (b) hemerythrin-like (H-HxxxE-H-HxxxE); and, (c) metazoan F-box proteins (H-HExxE-H-HxxxE). Interestingly, all but two hemerythrin-like families exhibit internal sequence and structural symmetry, suggesting that a duplication event may have led to the origin of the hemerythrin domain.
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