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Molecular Paradigm Iconoclasm

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 15 July 2025 | Viewed by 389

Special Issue Editor

Special Issue Information

Dear Colleagues,

The molecular sciences involve theoretical pillars, mechanistic paradigms that explain multiple phenomena in the biochemical and inorganic spaces. However, in time, many mechanistic explanations are found to be either incomplete or plainly incorrect. One example is the concept that DNA and RNA only exist to produce proteins rather than also serving as key cellular messaging molecules. Another was the notion that carbon monoxide (CO)-releasing molecules (CORMs) only exerted their effects via CO binding to heme groups attached to ion channels or molecules such as venom enzymes, instead of modifying proteins via CO-independent mechanisms. This Special Issue invites original works or review articles that describe novel mechanisms that challenge accepted paradigms of molecular interactions. A focus on biochemical paradigms is of special interest.

Prof. Dr. Vance G. Nielsen
Guest Editor

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Keywords

  • paradigm shift
  • biochemistry
  • cell signaling
  • coagulation
  • toxinology

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Published Papers (1 paper)

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17 pages, 3447 KiB  
Article
Carbon Monoxide or Ruthenium: Will the Real Modulator of Coagulation and Fibrinolysis Please Stand Up!
by Vance G. Nielsen and Anthony R. Abeyta
Int. J. Mol. Sci. 2025, 26(8), 3567; https://doi.org/10.3390/ijms26083567 - 10 Apr 2025
Viewed by 256
Abstract
The discovery of carbon monoxide releasing molecules (CORMs) was one of the most impactful innovations in biochemistry, affecting multiple disciplines for the past few decades. Sixteen years ago, a ruthenium dimer-containing CORM, CORM-2, enhanced coagulation and diminished fibrinolysis in human plasma by modulation [...] Read more.
The discovery of carbon monoxide releasing molecules (CORMs) was one of the most impactful innovations in biochemistry, affecting multiple disciplines for the past few decades. Sixteen years ago, a ruthenium dimer-containing CORM, CORM-2, enhanced coagulation and diminished fibrinolysis in human plasma by modulation of fibrinogen, plasmin, and α2-antiplasmin via CO binding to putative heme groups attached to these proteins. This finding linked CO exposure in settings involving heme oxygenase-1 upregulation during inflammation or environmental exposure to thromboembolic disease in hundreds of subsequent manuscripts. However, CO-independent effects of CORM-2 involving a putative ruthenium radical (Ru•) formed during CO release was found to be responsible for many of effects by CORM-2 in other works. Using a novel approach with human plasmatic coagulation kinetic methods, Ru• was posited to bind to critical histidines and other amino acids to modulate function, and excess histidine to quench CORM-2-mediated effects. This paradigm of histidine addition would definitively address if CO or Ru• was responsible for CORM-2-mediated effects. Thus, plasma coagulation/fibrinolytic kinetic data were assessed via thrombelastography ±CORM-2, ±histidine added. Histidine nearly completely abrogated CORM-2-mediated hypercoagulation in a concentration-dependent fashion; further, histidine also nearly eliminated all kinetic effects on fibrinolysis. In conclusion, CORM-2 Ru• formation, not CO release, is the true molecular mechanism modulating coagulation and fibrinolysis. Full article
(This article belongs to the Special Issue Molecular Paradigm Iconoclasm)
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