The Fully Oxidized State of the Glutamate Coordinated O₂-Tolerant [NiFe]-Hydrogenase Shows a Ni(III)/Fe(III) Open-Shell Singlet Ground State.

ABSTRACT: The oxygen tolerance of the [NiFe]-hydrogenase from H. thermoluteolus was recently assigned to originate from an unusual coordination sphere of the active site nickel atom (Shomura et al. Science 2017, 357, 928-932, 10.1126/science.aan4497). In the oxidized state, a terminal cysteine residue is displaced by a bidentate coordinating nearby Glu32 and thus moves to occupy a third μ-cysteine bridging position. Spectral features of the oxidized state were assigned to originate from a closed-shell Ni(IV)/Fe(II) state (Kulka-Peschke et al. J. Am. Chem. Soc. 2022, 144, 17022-17032, 10.1021/jacs.2c06400). Such a high-valent nickel oxidation state is unprecedented in biological systems. The spectral properties and the coordination sphere of that [NiFe]-hydrogenase can, however, also be rationalized by an energetically lower broken-symmetry Ni(III)/Fe(III) state of the active site which was not considered. In this open-shell singlet, the ligand-mediated antiferromagnetic spin-coupling leads to an overall S = 0 spin state with evenly distributed spin densities over the metal atoms. Experiments are suggested that may clarify the final assignment of redox states.

SUBMITTER: Kumar R 

PROVIDER: S-EPMC10214449 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature