When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase

Ciaccafava, Alexandre; Tombolelli, Daria; Domnik, Lilith; Fesseler, Jochen; Jeoung, Jae‐Hun; Dobbek, Holger; Mroginski, María Andrea; Zebger, Ingo; Hildebrandt, Peter

doi:10.1039/c5sc04554a

Cited by 24 publications

(46 citation statements)

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“…[9] Theactive role of C red2 state of the C-cluster in the reduction of NCO À to CN À was emphasized by two control experiments (see Figure S2 in the Supporting Information). [9] Additional control experiments were carried out to exclude CN À as ac ontaminant of the NCO À or as product of NCO À reduction to CN À mediated by possibly released metals ions (FeorNi) from the enzyme (see Figure S2). [9] Additional control experiments were carried out to exclude CN À as ac ontaminant of the NCO À or as product of NCO À reduction to CN À mediated by possibly released metals ions (FeorNi) from the enzyme (see Figure S2).…”

Section: In Memory Of Günther Felix Zebgermentioning

confidence: 99%

“…[9] Whereas in the C red1 state,o nly proton transfer to the solution is possible,t he directionality is reversed in the C red2 state to provide protons for the degradation of CO 2 to CO. [9] Whereas in the C red1 state,o nly proton transfer to the solution is possible,t he directionality is reversed in the C red2 state to provide protons for the degradation of CO 2 to CO.…”

Section: In Memory Of Günther Felix Zebgermentioning

confidence: 99%

“…Interactions with the terminal OH x ligand of the nearby Fe 1 ion are essential for CO turnover and subsequent oxidation to CO 2 with formation of the two-electron-reduced C red2 state. [9] Theactive role of C red2 state of the C-cluster in the reduction of NCO À to CN À was emphasized by two control experiments (see Figure S2 in Communications 7398 2017 Wiley-VCH Verlag GmbH &C o. KGaA, Weinheim Angew.C hem. [4] Despite alarge number of biochemical, spectroscopic,and crystallographic investigations,the detailed mechanism of the catalytic process of CODH remains unclear.…”

mentioning

confidence: 99%

“…[4] Despite alarge number of biochemical, spectroscopic,and crystallographic investigations,the detailed mechanism of the catalytic process of CODH remains unclear. [9] Additional control experiments were carried out to exclude CN À as ac ontaminant of the NCO À or as product of NCO À reduction to CN À mediated by possibly released metals ions (FeorNi) from the enzyme (see Figure S2). While CN À has been widely studied as an analogue for CO, [5] much less work has been reported on the binding of cyanate (NCO À ), which is considered to be an analogue of CO 2 .…”

mentioning

confidence: 99%

“…[7] TheI R spectrum obtained from these samples displayed two bands in the region between 2270 and 2000 cm À1 .T he band at 2168 cm À1 (2110 cm À1 with N 13 CO À )i sr eadily attributed to the stretching mode of NCO À in solution (Figure 1). [9] Theactive role of C red2 state of the C-cluster in the reduction of NCO À to CN À was emphasized by two control experiments (see Figure S2 in Communications 7398 2017 Wiley-VCH Verlag GmbH &C o. KGaA, Weinheim Angew.C hem. [9] Theactive role of C red2 state of the C-cluster in the reduction of NCO À to CN À was emphasized by two control experiments (see Figure S2 in Communications 7398 2017 Wiley-VCH Verlag GmbH &C o. KGaA, Weinheim Angew.C hem.…”

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Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide

et al. 2017

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The biocatalytic function of carbon monoxide dehydrogenase (CODH) has a high environmental relevance owing to its ability to reduce CO . Despite numerous studies on CODH over the past decades, its catalytic mechanism is not yet fully understood. In the present combined spectroscopic and theoretical study, we report first evidences for a cyanate (NCO ) to cyanide (CN ) reduction at the C-cluster. The adduct remains bound to the catalytic center to form the so-called CN -inhibited state. Notably, this conversion does not occur in crystals of the Carboxydothermus hydrogenoformans CODH enzyme (CODHII ), as indicated by the lack of the corresponding CN stretching mode. The transformation of NCO , which also acts as an inhibitor of the two-electron-reduced C state of CODH, could thus mimic CO turnover and open new perspectives for elucidation of the detailed catalytic mechanism of CODH.

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Section: In Memory Of Günther Felix Zebgermentioning

confidence: 99%

Section: In Memory Of Günther Felix Zebgermentioning

confidence: 99%

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confidence: 99%

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Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide

et al. 2017

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Die Kohlenmonoxid‐Dehydrogenase reduziert Cyanat zu Cyanid

et al. 2017

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Die Kohlenmonoxid-Dehydrogenase (CODH) hat eine hohe Umweltrelevanz aufgrund ihrer Fähigkeit, CO 2 biokatalytischzureduzieren. Trotz intensiver Bemühungen in den vergangenen Jahrzehnten ist der katalytische Mechanismus der CODH nochn ichtv ollständig aufgeklärt. In einer spektroskopischen und theoretischen Studie präsentieren wir nun erste Beweise füreine Reduktion von Cyanat (NCO À )zu Cyanid (CN À )a mC -Cluster.D as Addukt bleibt am katalyti-schenZ entrum gebunden und bildet den so genannten CN Àinhibierten Zustand. Interessanterweise findet diese Umwandlung nicht in Kristallen von CODHII Ch statt, was anhand des Fehlens der entsprechenden CN-Streckschwingungsbanden belegt werden kann. Die Transformation von NCO À ,e ines Inhibitors des C red2 -Zustands der CODH, kçnnte den CO 2 -Umsatz nachahmen und auf diese Weise neue Perspektiven für die Aufklärung des genauen katalytischen Mechanismus der CODH bieten. Die Kohlenmonoxid-Dehydrogenase (CODH) katalysiert die reversible Umwandlung zwischen CO und CO 2. Des Weiteren ist CODH ein zentrales Enzym des reduktiven Acetyl-CoA-Weges,w odurch es Mikroorganismen wie Carboxydothermus hydrogenoformans (Ch)u nd Moorella thermoacetica erlaubt, H 2 und CO 2 als Elektronen-und Kohlenstoffquelle zu nutzen oder CO zu oxidieren, um es als Elektronenquelle zu verwenden. [1] Die Rückreaktion, nämlich die enzymatische Reduktion von CO 2 ,i st von besonderem Interesse,d as ie als Vorlage fürd ie bioinspirierte Entwicklung von Katalysatoren fürden CO 2 -Abbau dienen kann. Das Enzym besteht aus zwei monomeren Einheiten, jede von ihnen beinhaltet drei Eisen-Schwefel-Cluster (D,Bund C, ausgehend von der Proteinoberfläche hin zum Inneren des Proteins). Der cubanfçrmige [4Fe-4S]-d-Cluster wird von jeweils zwei Cysteinresten pro Untereinheit koordiniert. Somit weist das homodimere Enzym einen d-Cluster, zwei B-Cluster und zwei [NiFe 4 S 4 OH x ]aktive Zentren (C-Cluster) auf.Es Abbildung 1. Bei 10 8 8Ci nLçsung gemesseneI R-Spektrend er CODHII Ch nach Inkubation mit NCO À (A) oder N 13 CO À (B).Abbildung 2. Bei 10 8 8CinLçsung gemesseneIR-Spektren der CODHII Ch ,i nkubiert mit NCO À bei pH 6.0 (A), pH 8.0 (B) und pH 10.0 (C). Einschub:N ormierte Intensitätder CN-Streckschwingungsbande als Funktion des pH-Werts. Der Pufferaustausch führte experimentabhängig zu Variationen der NCO À -Restkonzentration.

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Stepwise O₂‐Induced Rearrangement and Disassembly of the [NiFe₄(OH)(μ₃‐S)₄] Active Site Cluster of CO Dehydrogenase

et al. 2023

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Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of carbon dioxide to carbon monoxide. CODHs are found in anaerobic microorganisms and can rapidly lose their activity when exposed to air. What causes the loss of activity is unclear. In this study, we analyzed the timedependent structural changes induced by the presence of air on the metal centers of CODH-II. We show that inactivation is a multistep process. In a reversible step, the open coordination site on the Ni ion is blocked by a Ni,Fe-bridging μ-sulfido or chlorido ligand. Blocking this open coordination site with a cyanide ligand stabilizes the cluster against O 2 -induced decomposition, indicating that O 2 attacks at the Ni ion. In the subsequent irreversible phase, nickel is lost, the Fe ions rearrange and the sulfido ligands disappear. Our data are consistent with a reversible reductive reactivation mechanism to protect CODHs from transient overoxidation.

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When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase

Abstract: An integral approach including experimental and theoretical analysis has been carried out with the wild-type and engineered CODHIICh variant to assess the parameters that control the CN stretching frequency.

Cited by 24 publications

References 40 publications

Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide

Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide

Die Kohlenmonoxid‐Dehydrogenase reduziert Cyanat zu Cyanid

Stepwise O₂‐Induced Rearrangement and Disassembly of the [NiFe₄(OH)(μ₃‐S)₄] Active Site Cluster of CO Dehydrogenase

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When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase

Abstract: An integral approach including experimental and theoretical analysis has been carried out with the wild-type and engineered CODHIICh variant to assess the parameters that control the CN stretching frequency.

Cited by 24 publications

References 40 publications

Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide

Carbon Monoxide Dehydrogenase Reduces Cyanate to Cyanide

Die Kohlenmonoxid‐Dehydrogenase reduziert Cyanat zu Cyanid

Stepwise O2‐Induced Rearrangement and Disassembly of the [NiFe4(OH)(μ3‐S)4] Active Site Cluster of CO Dehydrogenase

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Stepwise O₂‐Induced Rearrangement and Disassembly of the [NiFe₄(OH)(μ₃‐S)₄] Active Site Cluster of CO Dehydrogenase