全細胞条件下におけるHクラスターの安定性：H様状態の形成と酸素に対する反応性
The [FeFe]-hydrogenase enzyme catalyzes reversible H2 oxidation using a hexanuclear iron cofactor known as the H-cluster, which exhibits exceptional catalytic performance but is highly sensitive to oxygen. Under in vitro conditions, oxygen-stable H-cluster forms can be generated through sulfide treatment under oxidizing conditions. This study demonstrates that an H-like species arises spontaneously within intact cells over a period of hours, coinciding with cessation of H2 production. Supplementation with cysteine or sulfide during enzyme maturation accelerates formation of this H-cluster state. Furthermore, both steric factors and proton transfer pathways were found to influence the formation of the H-like species, highlighting the significance of outer coordination sphere interactions in governing H-cluster reactivity.
An H-like state of the H-cluster forms spontaneously under intracellular conditions; its reactivity is governed by steric factors and outer coordination sphere proton transfer, with cysteine or sulfide promoting this transition.
This is basic research at the cellular or molecular level. For human application, inhalation is the most promising delivery route, but inhalation carries explosion risk and concentration matters (empirical LFL of 10%; high-concentration devices are not recommended).
See also:
https://h2-papers.org/en/papers/35258679