ArticleBiochemistry2025
Provision of a Redox Donor to Oxy-Ferrous PrnB Is Required for Pyrrolnitrin Synthesis.
R Brian McMillan, Hannah E Gering, Anastasia E Ledinina, Shan Xue, Sayali Karandikar, Shuangjun Lin, Garim You, Tzu-Yu Chen, Yisong Guo, Wei-Chen Chang and 1 more
Abstract read
In one paragraphArticle in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
2 · The registryThe trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
11 authors.
R Brian McMillanDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Hannah E GeringDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Anastasia E LedininaDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Shan XueDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.
Sayali KarandikarDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Shuangjun LinState Key Laboratory of Microbial Metabolism, Joint International Laboratory on Metabolic and Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.ORCID 0000-0001-9406-9233 Garim YouDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Tzu-Yu ChenDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.
Yisong GuoDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, United States.ORCID 0000-0002-4132-3565 Wei-Chen ChangDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.ORCID 0000-0002-2341-9846 Thomas M MakrisDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, United States.ORCID 0000-0001-7927-620X Funding
Understanding How Nonheme Iron-Dependent Enzymes Assemble Pharmacophores: Studies of Cyclopropane, Aziridine, and Isonitrile FormationR01GM127588 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI Wei-chen Chang · 2018 to 2026
$3.3MElucidate Mechanisms of Quinolone Alkaloid Biosynthesis via Iron(II)/2-Oxoglutarate Dependent Enzymes: Diverse, but Controlled ReactivityR01GM125924 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI Yisong Guo · 2018 to 2026
$3.3MDivergence of Carboxylate-Bridged Diiron Enzymes for Natural Product BiosynthesisR01GM135315 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI MAKRIS, THOMAS M · 2019 to 2022
$1.4MNIGMS NIH HHS R01 GM125924NIGMS NIH HHS R01 GM127588NIGMS NIH HHS R01 GM135315
6 · The paper itselfAbstract
PrnB, a long-standing member of the recently reclassified heme-dependent aromatic oxygenase (HDAO) superfamily of histidine-ligated heme enzymes, catalyzes the conversion of 7-chloro-l-tryptophan (7-Cl-Trp) to monodechloroaminopyrrolnitrin (MCAP). This unique ring rearrangement is an essential step in the biosynthesis of the broad-spectrum antifungal pyrrolnitrin. The conversion of 7-Cl-Trp to MCAP by PrnB differs from other HDAOs, which typically affect the mono- or dioxygenation of aromatic substrates. However, the molecular basis for this transformation has remained enigmatic due to the inability to reconstitute enzymatic activity
Indexed as
OxygenasesPyrrolnitrinKineticsOxidation-ReductionOxygenTryptophanOxygenOxygenasesPyrrolnitrinTryptophan
Identifiers
PMID40827054
PMCPMC13010262
What OpenQuestion holds
Textmetadata
LicenceTDM
Read underepoch 390