Wie der [NiFe4S4]‐Cluster der CO‐Dehydrogenase CO2 und NCO− aktiviert

Fesseler, Jochen; Jeoung, Jae‐Hun; Dobbek, Holger

doi:10.1002/ange.201501778

Cited by 21 publications

(4 citation statements)

References 35 publications

(10 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The crystal structure of substrate loaded Ni-CODH (EC 1.2.99.2) at atomic resolution has recently been reported [155]. From these data it becomes clear that carbon dioxide attached to the active site can form a two-electron reduced intermediate CO 2 2-in the enzymatic reaction mechanism (Fig.…”

Section: Photocatalytic Enzyme Models For Co 2 Reductionmentioning

confidence: 94%

“…Acceleration of such a two-electron substrate reduction is essential for the overall efficiency of the enzymatic process. While a moderately low reduction potential of E° = -0.53 V is required for this multielectron redox process [155], the uncatalyzed one-electron reduction of CO 2 would require a much more negative potential (E° = -1.90 V vs. NHE at pH = 7), by far exceeding the limiting constraints of biological systems (see section 4.1). Protonation of the two-electron reduced intermediate CO 2 2-could either lead to the production of formate (HCO 2 -) as a permanent product or, as is the case with Ni-CODH, to a fragmentation into OH -and CO.…”

Section: Photocatalytic Enzyme Models For Co 2 Reductionmentioning

confidence: 99%

“…Substrate binding at the multinuclear nickel-iron active site (C-cluster) of the bacterial enzyme Ni-CODH[155]. The carbon atom of the CO 2 molecule is coordinated to a nucleophilic Ni center.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The concept of photochemical enzyme models – State of the art

Knör

2016

Coordination Chemistry Reviews

View full text Add to dashboard Cite

Section: Photocatalytic Enzyme Models For Co 2 Reductionmentioning

confidence: 94%

Section: Photocatalytic Enzyme Models For Co 2 Reductionmentioning

confidence: 99%

See 1 more Smart Citation

The concept of photochemical enzyme models – State of the art

Knör

2016

Coordination Chemistry Reviews

View full text Add to dashboard Cite

“…[13] Such ad istinctiono ft he apparently equivalent elements in the Fe protein structure seems to be crucial for the activation andr eduction of CO 2 ;w hereas in the meantime, it may also account for the substantially lower activity of the Fe protein than the Nicontaining carbon monoxide dehydrogenase (Ni-CODH) in CO 2 reduction,a st he latter enzyme uses ar eal "asymmetric" His/ Lysp air (for Oc oordination) and ar eal "asymmetric" Fe/Ni pair (as Lewisa cid/base) at its active C-cluster site to facilitatet he cleavage of aC ÀOb ond. [26][27][28][29] Further investigations of the mechanism of CO 2 activation by Fe proteins,c ombined with comparisons with analogous systems, could shed additional light on the unique reactivity of scaffold-held FeS clusters toward CO 2 and facilitate future development of efficient FeS catalysts for ambient CO 2 conversion.…”

mentioning

confidence: 99%

Structural and Mechanistic Insights into CO₂ Activation by Nitrogenase Iron Protein

Rettberg

Stiebritz

Kang

et al. 2019

Chemistry A European J

View full text Add to dashboard Cite

The Fe protein of nitrogenase catalyzes the ambient reduction of CO2 when its cluster is present in the all‐ferrous, [Fe4S4]0 oxidation state. Here, we report a combined structural and theoretical study that probes the unique reactivity of the all‐ferrous Fe protein toward CO2. Structural comparisons of the Azotobacter vinelandii Fe protein in the [Fe4S4]0 and [Fe4S4]+ states point to a possible asymmetric functionality of a highly conserved Arg pair in CO2 binding and reduction. Density functional theory (DFT) calculations provide further support for the asymmetric coordination of O by the “proximal” Arg and binding of C to a unique Fe atom of the all‐ferrous cluster, followed by donation of protons by the proximate guanidinium group of Arg that eventually results in the scission of a C−O bond. These results provide important mechanistic and structural insights into CO2 activation by a surface‐exposed, scaffold‐held [Fe4S4] cluster.

show abstract

Die Kohlenmonoxid‐Dehydrogenase reduziert Cyanat zu Cyanid

et al. 2017

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Wie der [NiFe₄S₄]‐Cluster der CO‐Dehydrogenase CO₂ und NCO⁻ aktiviert

Cited by 21 publications

References 35 publications

The concept of photochemical enzyme models – State of the art

The concept of photochemical enzyme models – State of the art

Structural and Mechanistic Insights into CO₂ Activation by Nitrogenase Iron Protein

Die Kohlenmonoxid‐Dehydrogenase reduziert Cyanat zu Cyanid

Contact Info

Product

Resources

About

Wie der [NiFe4S4]‐Cluster der CO‐Dehydrogenase CO2 und NCO− aktiviert

Cited by 21 publications

References 35 publications

The concept of photochemical enzyme models – State of the art

The concept of photochemical enzyme models – State of the art

Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein

Die Kohlenmonoxid‐Dehydrogenase reduziert Cyanat zu Cyanid

Contact Info

Product

Resources

About

Wie der [NiFe₄S₄]‐Cluster der CO‐Dehydrogenase CO₂ und NCO⁻ aktiviert

Structural and Mechanistic Insights into CO₂ Activation by Nitrogenase Iron Protein