Infrapunases

Infrapunases are a proposed class of enzymes described as capable of catalyzing chemical transformations that are driven or modulated by infrared (IR) radiation. The term is not part of formal nomenclature in mainstream biochemistry, and as of now there is no widely accepted consensus that infrapunases constitute a distinct, universally recognized enzyme family. The concept appears mainly in speculative discussions and in a limited set of experimental reports exploring photobiocatalysis with infrared energy.

Proposed mechanisms for infrapunases often rely on specialized IR-absorbing chromophores or materials bound to or incorporated within an enzyme. These systems aim to harvest IR photons, convert the absorbed energy into chemical potential, and transfer it to the catalytic center. Hypothetical pathways include energy transfer from IR-absorbing cofactors to redox-active sites, upconversion processes that convert IR photons into higher-energy photons capable of driving standard catalytic steps, and localized heating or hot-electron effects that influence reaction barriers. Some designs invoke plasmonic or nanoparticle enhancers to boost IR absorption and energy delivery.

Research status and challenges are substantial. IR photons carry relatively low energy, so achieving efficient, selective catalysis under physiological or ambient conditions requires overcoming significant thermodynamic and kinetic barriers. Reported demonstrations often rely on high-intensity light sources and artificial constructs, and replication and standardization remain areas of ongoing scrutiny. If substantiated, infrapunases could influence fields such as photobiocatalysis, remote-control enzyme systems, and green chemistry, by enabling light-driven processes using the infrared portion of the spectrum.

See also: photobiocatalysis, photodynamic therapy, upconversion nanoparticles, infrared photochemistry.