Human Cells Can Make Their Own Hydrogen Gas, Groundbreaking Study Shows

Authors
Journal
Biochemical and Biophysical Research Communications
Year
DOI
10.1016/j.bbrc.2025.151596
Study Type
Human
Outcome
Positive
Peer Reviewed
Yes
Country
China
Health Condition
Cellular Metabolism Disorders
Body System
Cellular

TL;DR

Scientists have discovered that certain human and pig proteins can produce hydrogen gas, suggesting that this ability might be common in animals.

Key Finding

Mammalian cells contain [FeFe]-hydrogenase-like proteins capable of producing hydrogen gas in vitro, suggesting endogenous hydrogen production may be a widespread but previously unrecognized cellular process.

Summary

Researchers discovered that human and pig cells contain proteins similar to those found in algae that can produce hydrogen gas. When these proteins were made in bacteria and tested in the lab, they successfully produced hydrogen under oxygen-free conditions. The proteins were found throughout different tissues in both humans and pigs, suggesting that hydrogen production might be a basic cellular process that has been overlooked in evolution.

Practical Takeaway

This is very early laboratory research showing that mammalian cells may naturally produce hydrogen—it does not yet demonstrate that this happens in living organisms or that it has health benefits. Much more research is needed to understand whether endogenous hydrogen production occurs in the body and what role it might play in health.

Abstract

Although emerging evidence in mammals reveals that exogenously applied H2 positively regulates numerous physiological and pathological responses, it remains unclear whether and how mammalian cells produce H2 endogenously. Here, we report for the first time that recombinant human (Homo sapiens) and pig (Sus scrofa) nuclear prelamin recognition factor (Narf)-like proteins (also known as H. sapiens iron-only hydrogenase-like protein 1 [HsIOP1] and S. scrofa cytosolic iron-sulfur assembly component 3 [SsCIAO3], belonging to the [FeFe]-hydrogenase-like protein family), when expressed in a prokaryotic system, can potentially catalyze H2 production in vitro. Anaerobic induction was clearly observed. Further investigation of the transcriptome database revealed the widespread presence of these proteins in human and pig tissues. Sequence and structural analyses revealed that both HsIOP1 and SsCIAO3 may contain four conserved cysteine residues, forming a [4Fe4S] cluster, similar to the known [FeFe]-hydrogenase in Chlamydomonas reinhardtii. According to the observed hydrogenase activities of HsIOP1 and SsCIAO3 produced in Escherichia coli and the ubiquitous presence of Narf-like proteins in eukaryotic organisms, we propose that H2 production may be a universal phenomenon in eukaryotic organisms. Based on the results of the evolutionary tree, it was further hypothesized that hydrogen metabolism may have been ignored in the evolution and development of eukaryotic cells for a considerable time.