Influence of illumination on the electronic interaction between 77Se and nickel in active F420‐non‐reducing hydrogenase from Methanococcus voltae

Sorgenfrei, Oliver; Klein, Albrecht; Albracht, S.P.J.

doi:10.1016/0014-5793(93)80652-b

Cited by 45 publications

(51 citation statements)

References 41 publications

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“…To further identify the Cys residue that can be alkylated after H, activation, we have tried to repeat the alkylation experiment on a [NiFeSeIhydrogenase, where one of the sulfur ligands to Ni is replaced by the Se atom of a selenocysteine (He et al, 1989;Sorgenfrei et al, 1993). However, we have been unable to inhibit the activity of the D. baculatus [NiFeSeIhydrogenase by iodoacetamide.…”

Section: Discussionmentioning

confidence: 99%

“…Some Ni-containing hydrogenases contain Se in the form of a single selenocysteine in place of a cysteine, as shown for the first time for the '%e-labeled hydrogenase from Methanococcus vannielii (Yamazaki, 1982). This selenocysteine is in the coordination sphere of the Ni atom (He et al, 1989;Sorgenfrei et al, 1993 hydrogenases are closely related to the [NiFeIhydrogenases and have a high degree of amino-acid-sequence similarity (Voordouw, 1992). The hydrogenase of the purple sulfur photosynthetic bacterium Thiocapsa roseopersicina (Gogotov et al, 1978), similarly to most other [NiFeIhydrogenases, is composed of two subunits of approximately 60 kDa and 30 kDa (Sherman at al., 1991).…”

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confidence: 99%

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Inhibition by Iodoacetamide and Acetylene of the H‐D‐Exchange Reaction Catalyzed by Thiocapsa Roseopersicina Hydrogenase

Зорин

Dimon

Gagnon

et al. 1996

European Journal of Biochemistry

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The kinetics of H-D isotope exchange catalyzed by the thermostable hydrogenase from Thiocapsa roseopersicina have been studied by analysis of the exchange between D, and H,O. The pH dependence of the exchange reaction was examined between pH 2.5 and pH 11. Over the whole pH range, HD was produced at a higher initial velocity than H,, with a marked optimum at pH 5.5; a second peak in the pH profile was observed at around pH 8.5. The rapid formation of H, with respect to HD in the D,/H,O system is consistent with a heterolytic cleavage of D, into D' and an enzyme hydride that can both exchange with the solvent. The H-D-exchange activity was lower in the H,/D,O system than in the D,/ H,O system. The other reactions catalyzed by the hydrogenase, H, oxidation and H, evolution, are pH dependent; the optimal pH were 9.5 for H, uptake and 4.0 for H, production. Treatment of the active form of hydrogenase by iodoacetamide led to a slow and irreversible inhibition of the H-D exchange. When i~do[l-'~C]acetamide was incubated with hydrogenase, the radioactive labeling of the large subunit was higher for the enzyme activated under H, than for the inactive oxidized form. Cysteine residues were identified as the alkylated derivative by amino acid analysis. Acetylene, which inhibits H-D exchange and abolishes the Ni-C EPR signal, protected the enzyme from irreversible inhibition by iodoacetamide. These data indicate that iodoacetamide can reach the active site of the H,-activated hydrogenase from 7: roseopersicina. This was not found to be the case with the seleno hydrogenase from Desulfovibrio baculatus (now Desulfornicrobiurn baculatus). Cysteine modification by iodoacetamide upon activation of the enzyme concomitant with loss of H-D exchange indicates that reductive activation makes at least one Cys residue of the active site available for alkylation.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Inhibition by Iodoacetamide and Acetylene of the H‐D‐Exchange Reaction Catalyzed by Thiocapsa Roseopersicina Hydrogenase

Зорин

Dimon

Gagnon

et al. 1996

European Journal of Biochemistry

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“…In some enzymes this residue is replaced by selenocysteine. EPR spectra of these enzymes show hyperfine interaction from 77Se (I = 1/2), which is direct evidence for a Ni-Se bond (He et al, 1989;Sorgenfrei et al, 1993). The amino-terminal part of the large subunit contains two additional strictly conserved Cys residues in an RGxEx~&xCGxCxxxH motif.…”

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confidence: 92%

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Bagley

Duin²,

Roseboom³

et al. 1995

Biochemistry

215

217

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An infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from Chromatium vinosum Bagley, K.A.; Duin, E.L.; Roseboom, W.; Albracht, S.P.J.; Woodruff, W.H. General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. ABSTRACT: Fourier transform infrared studies of nickel hydrogenase from Chromatium vinosum reveal the presence of a set of three absorption bands in the 2100-1900 cm-1 spectral region. These bands, which do not arise from carbon monoxide, have line widths and intensities rivaling those of a band arising from the carbon monoxide stretching frequency (v(C0)) in the Ni(I1)CO species of this enzyme

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“…This spectrum resembles a signal which was obtained upon reductive activation of oxidized hydrogenases from different origins [4, 17-19, 25, 261. The species exhibiting this signal are light sensitive at low temperatures [23,251. Illumination with white light led to disappearance of the signal, and concomitantly a new signal with its lowest g value at 2.05 was observed.…”

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confidence: 93%

Changes in the Electronic Structure Around Ni in Oxidized and Reduced Selenium‐Containing Hydrogenases from Methanococcus Voltae

Sorgenfrei

Duin

Klein

et al. 1997

European Journal of Biochemistry

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The selenium-containing F420-reducing hydrogenase from Methanococcus voltae was anaerobically purified to a specific hydrogen-uptake activity of 350 U/mg protein as determined with the natural electron acceptor. The concentrated enzyme was used for EPR-spectroscopic investigations. As isolated, the enzyme showed an EPR spectrum with gnyL values of 2.21, 2.15 and 2.01. Illumination of such samples at low temperatures led to an EPR spectrum with gxyz values of 2.05, 2.11 and 2.29. These spectra are typical for [NiFeIhydrogenases in the active state. Spectra of samples enriched in 77Se showed a hyperfine interaction between the unpaired spin of the nickel ion and the nuclear spin of one "Se atom before and after illumination. A 90" flip of the electronic z-axis is proposed to explain the hyperfine interaction in both states. This has been demonstrated previously only for the F420-non-reducing hydrogenase from M . voltue, where the selenium atom is present as a selenocysteine residue on an unusuallyThe results demonstrate that the three-dimensional structures of the active sites in the selenium-containing F420-reducing and F420-non-reducing hydrogenases from M. voltue are highly similar and hence are not influenced by the unusual subunit structure of the latter enzyme. Oxidized samples containing either natural selenium or 77Se were prepared from the F420-reducing and the selenium-containing F420-nonreducing hydrogenase. Both enzymes exhibited EPR spectra typical for [NiFeIhydrogenases in the inactive 'ready' state. In contrast to the reduced form, no splitting of the nickel-derived signal due to the nuclear spin of "Se was observed in the oxidized state, indicating that the electronic z-axis is perpendicular to the Ni-Se direction.Keywords: [NiFeIhydrogenase ; EPR ; purification ; selenium ; selenocysteine.The simplest biochemical redox reaction, namely the reversible, heterolytic cleavage of dihydrogen into two protons and two electrons is catalysed by enzymes called hydrogenases [I, 21. These are found in many organisms from all three domains, bacteria, eukarya and archaea. Different classes are defined according to the metal content of the enzymes. One class comprises hydrogenases containing no metal other than iron. These enzymes are called Fe-only hydrogenases or [Felhydrogenases [l]. The second class consists of hydrogenases that contain nickel in addition to iron. Accordingly these enzymes were named [NiFeIhydrogenases. Most of the characterized hydrogenases belong to this group. The EPR spectra of nickel respond to redox changes [4-71 and this M. voltae is an anaerobic archaeon that gains energy by oxidation of hydrogen via hydrogenases and concomitant reduction Correspondence to 0. Sorgenfrei,

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Influence of illumination on the electronic interaction between ⁷⁷Se and nickel in active F₄₂₀‐non‐reducing hydrogenase from Methanococcus voltae

Cited by 45 publications

References 41 publications

Inhibition by Iodoacetamide and Acetylene of the H‐D‐Exchange Reaction Catalyzed by Thiocapsa Roseopersicina Hydrogenase

Inhibition by Iodoacetamide and Acetylene of the H‐D‐Exchange Reaction Catalyzed by Thiocapsa Roseopersicina Hydrogenase

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Changes in the Electronic Structure Around Ni in Oxidized and Reduced Selenium‐Containing Hydrogenases from Methanococcus Voltae

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