How Hydrogen Acts as Antioxidant Through Iron in Blood Proteins
- Authors
- Song-Ae Kim, Yu-Chol Jong, Myong-Su Kang, Chol-Jun Yu
- Journal
- Journal of Molecular Modeling
- Year
- 2022
- DOI
- 10.1007/s00894-022-05264-y
- Study Type
- Molecular Assay
- Outcome
- Positive
- Peer Reviewed
- Yes
- Country
- North Korea
- Health Condition
- Oxidative Stress
- Body System
- Cardiovascular
TL;DR
Scientists used computer simulations to show how molecular hydrogen can act as an antioxidant by interacting with a component of hemoglobin in a way that could help neutralize harmful molecules in the body.
Key Finding
Protoheme acts as a biological catalyst that lowers the energy barrier needed for hydrogen to neutralize reactive oxygen and nitrogen species by more than 40% compared to free hydrogen molecules.
Summary
This study used computer modeling to understand how molecular hydrogen might work as an antioxidant (a substance that neutralizes harmful molecules) in the body. Researchers simulated how hydrogen interacts with protoheme, an iron-containing compound found in blood, and how this interaction could neutralize reactive oxygen and nitrogen species (unstable molecules that damage cells). The calculations showed that protoheme acts as a catalyst (a substance that speeds up chemical reactions), making it easier for hydrogen to neutralize these harmful molecules than it would be on its own.
Practical Takeaway
This is a theoretical computer study, not an experiment in living organisms or people, so it cannot directly confirm that hydrogen water provides antioxidant benefits. The findings suggest a plausible mechanism for how hydrogen might work at the molecular level, but actual human studies would be needed to determine whether hydrogen water has meaningful health effects.
Abstract
Recently, molecular hydrogen has been found to exhibit antioxidation activity through many clinical experiments, but the mechanism has not been fully understandable at atomic level. In this work, we perform systematic ab initio calculations of protoheme-hydrogen complexes to clarify the antioxidation mechanism of molecular hydrogen. We make molecular modeling of iron-protoporphyrin coordinated by imidazole, FeP(Im), and its hydrogen as well as dihydrogen complexes, together with reactive oxygen/nitrogen species (RONS). We carry out structural optimization and Mulliken charge analysis, revealing the two kinds of bonding characteristics between FeP(Im) and H[Formula: see text]: dihydrogen bonding in the end-on asymmetric configuration and Kubas bonding in the side-on symmetric configuration of H[Formula: see text] molecule. The activation barriers for adsorption and dissociation of H[Formula: see text] on and further desorption of H atom from FeP(Im) are found to be below 2.78 eV at most, which is remarkably lower than the H-H bond breaking energy of 4.64 eV in free H[Formula: see text] molecule. We find that the hydrogen bond dissociation energies of FeP(Im)-H[Formula: see text] and -H complexes are lower than those of RONS-H complexes, indicating the decisive role of protoheme as an effective catalyst in RONS antioxidation by molecular hydrogen in vivo.