Spectroscopic and Electrochemical Characterization of the [NiFeSe] Hydrogenase from <i>Desulfovibrio vulgaris</i> Miyazaki F: Reversible Redox Behavior and Interactions between Electron Transfer Centers

Riethausen, Jana; Rüdiger, Olaf; Gärtner, Wolfgang; Lubitz, Wolfgang; Shafaat, Hannah S.

doi:10.1002/cbic.201300120

Cited by 18 publications

(31 citation statements)

References 67 publications

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“…The enzymes belonging to the subfamily of [NiFeSe] hydrogenases are special because they have a fast H 2 production rate [5][6][7]. Compared to [NiFeS] hydrogenases, the Se enzyme records a higher H 2 production activity [8].…”

Section: Introductionmentioning

confidence: 99%

Probing the Structure of [NiFeSe] Hydrogenase with QM/MM Computations

et al. 2020

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The geometry and vibrational behavior of selenocysteine [NiFeSe] hydrogenase isolated from Desulfovibrio vulgaris Hildenborough have been investigated using a hybrid quantum mechanical (QM)/ molecular mechanical (MM) approach. Structural models have been built based on the three conformers identified in the recent crystal structure resolved at 1.3 Å from X-ray crystallography. In the models, a diamagnetic Ni2+ atom was modeled in combination with both Fe2+ and Fe3+ to investigate the effect of iron oxidation on geometry and vibrational frequency of the nonproteic ligands, CO and CN-, coordinated to the Fe atom. Overall, the QM/MM optimized geometries are in good agreement with the experimentally resolved geometries. Analysis of computed vibrational frequencies, in comparison with experimental Fourier-transform infrared (FTIR) frequencies, suggests that a mixture of conformers as well as Fe2+ and Fe3+ oxidation states may be responsible for the acquired vibrational spectra.

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Section: Introductionmentioning

confidence: 99%

Probing the Structure of [NiFeSe] Hydrogenase with QM/MM Computations

et al. 2020

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“…There is IR spectroscopic evidence for the Ni a -C and Ni a -R states of the active site, 79,80 and Ni a -L states have been observed by EPR spectroscopy upon illumination at cryogenic temperatures. 80,81 …”

Section: Introductionmentioning

confidence: 99%

Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy

2017

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Catalysis of H2 production and oxidation reactions is critical in renewable energy systems based around H2 as a clean fuel, but the present reliance on platinum-based catalysts is not sustainable. In nature, H2 is oxidized at minimal overpotential and high turnover frequencies at [NiFe] catalytic sites in hydrogenase enzymes. Although an outline mechanism has been established for the [NiFe] hydrogenases involving heterolytic cleavage of H2 followed by a first and then second transfer of a proton and electron away from the active site, details remain vague concerning how the proton transfers are facilitated by the protein environment close to the active site. Furthermore, although [NiFe] hydrogenases from different organisms or cellular environments share a common active site, they exhibit a broad range of catalytic characteristics indicating the importance of subtle changes in the surrounding protein in controlling their behavior. Here we review recent time-resolved infrared (IR) spectroscopic studies and IR spectroelectrochemical studies carried out in situ during electrocatalytic turnover. Additionally, we re-evaluate the significant body of IR spectroscopic data on hydrogenase active site states determined through more conventional solution studies, in order to highlight mechanistic steps that seem to apply generally across the [NiFe] hydrogenases, as well as steps which so far seem limited to specific groups of these enzymes. This analysis is intended to help focus attention on the key open questions where further work is needed to assess important aspects of proton and electron transfer in the mechanism of [NiFe] hydrogenases.

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“…[ 11 ] In the O 2 oxidized [NiFeSe] hydrogenase, however, the nickel center is not oxidized and no bridging ligand is observed between the two metal centers. [ 7g , 12 ] Crystallographic evidence suggests that it is the Sec selenium and, in some cases, Cys sulfur that is oxidized in [NiFeSe] hydrogenases. [ 12c , d , 13 ]…”

Section: Introductionmentioning

confidence: 99%

Synthetic Active Site Model of the [NiFeSe] Hydrogenase

Wombwell

Reisner

2015

Chemistry A European J

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A dinuclear synthetic model of the [NiFeSe] hydrogenase active site and a structural, spectroscopic and electrochemical analysis of this complex is reported. [NiFe(‘S2Se2’)(CO)3] (H2‘S2Se2’=1,2-bis(2-thiabutyl-3,3-dimethyl-4-selenol)benzene) has been synthesized by reacting the nickel selenolate complex [Ni(‘S2Se2’)] with [Fe(CO)3bda] (bda=benzylideneacetone). X-ray crystal structure analysis confirms that [NiFe(‘S2Se2’)(CO)3] mimics the key structural features of the enzyme active site, including a doubly bridged heterobimetallic nickel and iron center with a selenolate terminally coordinated to the nickel center. Comparison of [NiFe(‘S2Se2’)(CO)3] with the previously reported thiolate analogue [NiFe(‘S4’)(CO)3] (H2‘S4’=H2xbsms=1,2-bis(4-mercapto-3,3-dimethyl-2-thiabutyl)benzene) showed that the selenolate groups in [NiFe(‘S2Se2’)(CO)3] give lower carbonyl stretching frequencies in the IR spectrum. Electrochemical studies of [NiFe(‘S2Se2’)(CO)3] and [NiFe(‘S4’)(CO)3] demonstrated that both complexes do not operate as homogenous H2 evolution catalysts, but are precursors to a solid deposit on an electrode surface for H2 evolution catalysis in organic and aqueous solution.

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Spectroscopic and Electrochemical Characterization of the [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Reversible Redox Behavior and Interactions between Electron Transfer Centers

Cited by 18 publications

References 67 publications

Probing the Structure of [NiFeSe] Hydrogenase with QM/MM Computations

Probing the Structure of [NiFeSe] Hydrogenase with QM/MM Computations

Proton Transfer in the Catalytic Cycle of [NiFe] Hydrogenases: Insight from Vibrational Spectroscopy

Synthetic Active Site Model of the [NiFeSe] Hydrogenase

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