ArticleInorganic chemistry2013
Porphyrin-substituted H-NOX proteins as high-relaxivity MRI contrast agents.
Article in Inorganic chemistry, 2013. 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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Who cites it
9 citing papers in PubMed, 43 citations in OpenAlex.
- The direct expression of apo heme proteins: A general strategy to obtain designer heme proteins with abiological cofactors.Methods in enzymology · 2025Article
- X-ray and nuclear spectroscopies to reveal the element specific oxidation states and electronic spin states for nanoparticulated manganese cyanidoferrates and analogs.Physchem (Basel, Switzerland) · 2024Article
- Corrole-protein interactions in H-NOX and HasA.RSC chemical biology · 2022Article
- De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Corrole-Substituted Fluorescent Heme Proteins.Inorganic chemistry · 2021Article
- The Red Color of Life Transformed - Synthetic Advances and Emerging Applications of Protoporphyrin IX in Chemical Biology.European journal of organic chemistry · 2020Review
- A novel thermophilic hemoprotein scaffold for rational design of biocatalysts.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Manganese(III) porphyrins complexed with P22 virus-like particles as T1-enhanced contrast agents for magnetic resonance imaging.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- A review of responsive MRI contrast agents: 2005-2014.Contrast media & molecular imagingReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Heme proteins are exquisitely tuned to carry out diverse biological functions while employing identical heme cofactors. Although heme protein properties are often altered through modification of the protein scaffold, protein function can be greatly expanded and diversified through replacement of the native heme with an unnatural porphyrin of interest. Thus, porphyrin substitution in proteins affords new opportunities to rationally tailor heme protein chemical properties for new biological applications. Here, a highly thermally stable Heme Nitric oxide/OXygen binding (H-NOX) protein is evaluated as a magnetic resonance imaging (MRI) contrast agent. T1 and T2 relaxivities measured for the H-NOX protein containing its native heme are compared to the protein substituted with unnatural manganese(II/III) and gadolinium(III) porphyrins. H-NOX proteins are found to provide unique porphyrin coordination environments and have enhanced relaxivities compared to commercial small-molecule agents. Porphyrin substitution is a promising strategy to encapsulate MRI-active metals in heme protein scaffolds for future imaging applications.
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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.