ReviewArchives of biochemistry and biophysics2026
Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.
Review in Archives of biochemistry and biophysics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
The 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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Nonheme iron enzymes encompass one of the most chemically versatile families of metalloenzymes, catalyzing an extraordinary range of oxidative transformations essential to metabolism, natural product biosynthesis, and environmental biodegradation. Despite their mechanistic diversity, these enzymes share a unifying principle: the controlled activation of molecular oxygen to drive selective substrate oxidation. Many mononuclear nonheme iron enzymes employ a conserved 2-His-1-carboxylate facial triad and frequently utilize 2-oxoglutarate (2OG) as a co-substrate to generate Fe(IV)O intermediates that mediate diverse C-H and CC bond oxidations. Organic cofactor-independent nonheme iron enzymes have been recognized for decades, with early examples including catechol dioxygenases and intradiol-cleaving enzymes. Structural and mechanistic advances over the past two decades have revealed that many of these cofactor-independent enzymes feature alternative 3-His or 4-His metal-binding motifs, which confer distinct electronic properties and enable oxygen activation pathways beyond those accessible to 2-His-1-carboxylate systems. Parallel advances in the study of dinuclear nonheme iron enzymes have illuminated equally rich mechanistic diversity, particularly within the ferritin-like (FDO) and heme-oxygenase-like (HDO) families. These diiron systems employ cooperative metal-metal interactions to form diiron-oxygen intermediates that enable multielectron oxidation chemistry beyond the reach of mononuclear centers. Structural and mechanistic studies of HDO-type enzymes involved in natural product biosynthetic pathways have revealed noncanonical coordination environments and substrate selectivity, underscoring the evolutionary and functional plasticity of nonheme iron catalysis. This review summarizes emerging insights into His-rich mononuclear enzymes and HDO-type diiron systems, highlighting their structural innovations, mechanistic principles, and collective contributions to expanding the frontiers of oxygen activation chemistry.
Indexed as
Identifiers
What OpenQuestion holds
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.