EPR and electron nuclear double resonance investigation of oxidized hydrogenase II (uptake) from Clostridium pasteurianum W5. Effects of carbon monoxide binding.

Telser, Joshua; Benecky, Michael J.; Adams, Michael W. W.; Mortenson, Leonard E.; Hoffman, Brian M.

doi:10.1016/s0021-9258(18)48282-8

Cited by 48 publications

(35 citation statements)

References 11 publications

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“…As our 57 Fe EPR data showed effective spin density on the H-cluster, we compared 1 H ENDOR spectra of R˙ ox with those of H ox , H ox –CO, and H hyd from different [FeFe]-hydrogenases. 45–47 As with the 57 Fe data, the strength of the hfis and the spectral shape of R˙ ox 1 H ENDOR resemble those detected with H ox –CO assigned to β-protons of the cysteine ligands of [4Fe] H . 45–47 …”

Section: Resultssupporting

confidence: 70%

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The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

et al. 2022

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Section: Resultssupporting

confidence: 70%

“… 45–47 As with the 57 Fe data, the strength of the hfis and the spectral shape of R˙ ox 1 H ENDOR resemble those detected with H ox –CO assigned to β-protons of the cysteine ligands of [4Fe] H . 45–47 …”

Section: Resultssupporting

confidence: 70%

The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

et al. 2022

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“…This difference spectrum was well simulated as an ENDOR doublet with A( 57 Fe) = 10.55 MHz. Both A( 57 Fe) values for HydA1 are consistent with previous ENDOR and Mössbauer spectroscopic studies of the H ox state of Desulfovibrio vulgaris and Clostridium pasteurianum hydrogenases (≈16 to 18 MHz for the [2Fe] H subcluster and ≈8 to 10 MHz for the [4Fe-4S] H cluster) (23)(24)(25)(26), although they differ somewhat from those derived from ENDOR data for the Desulfovibrio desulfuricans hydrogenase (12.4 and 11.1 MHz, respectively) (27). Comparing the magnitudes of the two A( 57 Fe) values determined above confirms that the greatest spin density of the H-cluster in the H ox state lies on the [2Fe] H subcluster.…”

supporting

confidence: 89%

The HydG Enzyme Generates an Fe(CO) ₂ (CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster

Kuchenreuther

Myers

Suess

et al. 2014

Science

110

208

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Three iron-sulfur proteins–HydE, HydF, and HydG–play a key role in the synthesis of the [2Fe]H component of the catalytic H-cluster of FeFe hydrogenase. The radical S-adenosyl-l-methionine enzyme HydG lyses free tyrosine to produce p-cresol and the CO and CN− ligands of the [2Fe]H cluster. Here, we applied stopped-flow Fourier transform infrared and electron-nuclear double resonance spectroscopies to probe the formation of HydG-bound Fe-containing species bearing CO and CN− ligands with spectroscopic signatures that evolve on the 1- to 1000-second time scale. Through study of the 13C, 15N, and 57Fe isotopologs of these intermediates and products, we identify the final HydG-bound species as an organometallic Fe(CO)2(CN) synthon that is ultimately transferred to apohydrogenase to form the [2Fe]H component of the H-cluster.

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“…Upon CO inhibition, spin exchange coupling is significantly enhanced in favor of the [4Fe-4S] cluster leading to an axial EPR spectrum with g = 2.05 and 2.01 in Hox-CO (Figure ). , The spin polarization was recently calculated to fit an apical CO model . Studying the 14 N hyperfine interactions, Silakov et al revealed the chemical nature of the dithiolate group resolving a long-running controversy whether its central atom is an oxygen (odt), carbon (pdt), or nitrogen atom (adt) in favor of the latter .…”

Section: Novel Methodsmentioning

confidence: 99%

Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations

et al. 2020

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Hydrogenases are redox enzymes that catalyze the conversion of protons and molecular hydrogen (H2). Based on the composition of the active site cofactor, the monometallic [Fe]hydrogenase is distinguished from the bimetallic [NiFe]-or [FeFe]-hydrogenase. The latter has been reported with particularly high turnover activities for both H2 release and H2 oxidation, notably at neutral pH, ambient temperatures, and negligible electric overpotential. Due to these properties, [FeFe]-hydrogenase represents the 'gold standard' in enzymatic hydrogen turnover.Understanding hydrogenase chemistry is crucial for the design of transition metal complexes that serve as potentially sustainable proton reduction or H2 oxidation catalysts, e.g. in electrolytic devices or fuel cells.Even 20 years after the crystal structures of [FeFe]-hydrogenase have been published, several aspects of biological hydrogen turnover are heatedly discussed. In this perspective, we give an overview on how the diversity of naturally occurring and artificially prepared, semi-synthetic [FeFe]-hydrogenases deepens our understanding of hydrogenase chemistry. In parallel, we cover recent results from biophysical techniques that go beyond the scope of conventional Xray diffraction, EPR, and FTIR spectroscopy. Taking into account both proton transfer and electron transfer as well as the notorious sensitivity of [FeFe]-hydrogenases towards carbon monoxide, the discussion further touches upon the molecular proceedings of biological hydrogen turnover.

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EPR and electron nuclear double resonance investigation of oxidized hydrogenase II (uptake) from Clostridium pasteurianum W5. Effects of carbon monoxide binding.

Cited by 48 publications

References 11 publications

The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

The HydG Enzyme Generates an Fe(CO) ₂ (CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster

Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations

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EPR and electron nuclear double resonance investigation of oxidized hydrogenase II (uptake) from Clostridium pasteurianum W5. Effects of carbon monoxide binding.

Cited by 48 publications

References 11 publications

The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

The oxygen-resistant [FeFe]-hydrogenase CbA5H harbors an unknown radical signal

The HydG Enzyme Generates an Fe(CO) 2 (CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster

Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations

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The HydG Enzyme Generates an Fe(CO) ₂ (CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster