The large subunit of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha - a minimal hydrogenase?

Chemical Science
Giorgio CasertaOliver Lenz

Abstract

Chemically synthesized compounds that are capable of facilitating the reversible splitting of dihydrogen into protons and electrons are rare in chemists' portfolio. The corresponding biocatalysts - hydrogenases - are, however, abundant in the microbial world. [NiFe]-hydrogenases represent a major subclass and display a bipartite architecture, composed of a large subunit, hosting the catalytic NiFe(CO)(CN)2 cofactor, and a small subunit whose iron-sulfur clusters are responsible for electron transfer. To analyze in detail the catalytic competence of the large subunit without its smaller counterpart, we purified the large subunit HoxC of the regulatory [NiFe]-hydrogenase of the model H2 oxidizer Ralstonia eutropha to homogeneity. Metal determination and infrared spectroscopy revealed a stoichiometric loading of the metal cofactor. This enabled for the first time the determination of the UV-visible extinction coefficient of the NiFe(CO)(CN)2 cofactor. Moreover, the absence of disturbing iron-sulfur clusters allowed an unbiased look into the low-spin Fe2+ of the active site by Mössbauer spectroscopy. Isolated HoxC was active in catalytic hydrogen-deuterium exchange, demonstrating its capacity to activate H2. Its catalytic activity ...Continue Reading

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Citations

Aug 23, 2020·International Journal of Molecular Sciences·Qin FanMatthias Gimpel
Apr 21, 2021·Dalton Transactions : an International Journal of Inorganic Chemistry·Meng-Hua LiMei-Jin Lin
Aug 21, 2021·Inorganic Chemistry·Martin BörnerBerthold Kersting

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Methods Mentioned

BETA
electron paramagnetic resonance
X-ray
nuclear
Protein Assay
size-exclusion chromatography

Software Mentioned

WMOSS4
GAUSSIAN16
Matlab
Easyspin
Bruker OPUS
Origin

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