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- Title
Stability of the H-cluster under whole-cell conditions—formation of an H<sub>trans</sub>-like state and its reactivity towards oxygen.
- Authors
Lorenzi, Marco; Ceccaldi, Pierre; Rodríguez-Maciá, Patricia; Redman, Holly Jayne; Zamader, Afridi; Birrell, James A.; Mészáros, Livia S.; Berggren, Gustav
- Abstract
Hydrogenases are metalloenzymes that catalyze the reversible oxidation of molecular hydrogen into protons and electrons. For this purpose, [FeFe]-hydrogenases utilize a hexanuclear iron cofactor, the H-cluster. This biologically unique cofactor provides the enzyme with outstanding catalytic activities, but it is also highly oxygen sensitive. Under in vitro conditions, oxygen stable forms of the H-cluster denoted Htrans and Hinact can be generated via treatment with sulfide under oxidizing conditions. Herein, we show that an Htrans-like species forms spontaneously under intracellular conditions on a time scale of hours, concurrent with the cells ceasing H2 production. Addition of cysteine or sulfide during the maturation promotes the formation of this H-cluster state. Moreover, it is found that formation of the observed Htrans-like species is influenced by both steric factors and proton transfer, underscoring the importance of outer coordination sphere effects on H-cluster reactivity.
- Subjects
STATE formation; METALLOENZYMES; COFACTORS (Biochemistry); IRON; ELECTRON paramagnetic resonance; HYDROGENASE; OXYGEN; SILVER sulfide
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2022, Vol 27, Issue 3, p345
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-022-01928-5