Characterization of the iron–sulfur clusters in the nitrogenase‐like reductase CfbC/D required for coenzyme F430 biosynthesis
Abstract: Coenzyme F430 is a nickel-containing tetrapyrrole, serving as the prosthetic group of methyl-coenzyme M reductase in methanogenic and methanotrophic archaea. During coenzyme F430 biosynthesis, the tetrapyrrole macrocycle is reduced by the nitrogenase-like CfbC/D system consisting of the reductase component CfbC and the catalytic component CfbD. Both components are homodimeric proteins, each carrying a [4Fe-4S] cluster. Here, the ligands of the [4Fe-4S] clusters of CfbC2 and CfbD2 were identified revealing an all cysteine ligation of both clusters. Moreover, the midpoint potentials of the [4Fe-4S] clusters were determined to be −256 mV for CfbC2 and −407 mV for CfbD2. These midpoint potentials indicate that the consecutive thermodynamically unfavorable 6 individual “up-hill” electron transfers to the organic moiety of the Ni2+-sirohydrochlorin a,c-diamide substrate require an intricate interplay of ATP-binding, hydrolysis, protein complex formation and release to drive product formation, which is a common theme in nitrogenase-like systems
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
The FEBS journal. - 291, 14 (2024) , 3233-3248, ISSN: 1742-4658
- Event
-
Veröffentlichung
- (where)
-
Freiburg
- (who)
-
Universität
- (when)
-
2024
- Creator
-
Ramos, José V.
Kulka‐Peschke, Catharina J.
Bechtel, Dominique F.
Zebger, Ingo
Pierik, Antonio J.
Layer, Gunhild
- DOI
-
10.1111/febs.17134
- URN
-
urn:nbn:de:bsz:25-freidok-2468979
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:45 PM CET
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Ramos, José V.
- Kulka‐Peschke, Catharina J.
- Bechtel, Dominique F.
- Zebger, Ingo
- Pierik, Antonio J.
- Layer, Gunhild
- Universität
Time of origin
- 2024
Other Objects (12)
Biosynthesis of iron-sulfur clusters and tetrapyrroles in microorganisms
Iron-sulfur clusters in chemistry and biology, Volume 2.. Biochemistry, biosynthesis and human diseases
Iron-sulfur clusters in chemistry and biology
The sulfur oxygenase reductase from Acidianus ambivalens : functional and structural characterization of a sulfur-disproportionating enzyme
Iron–Sulfur cluster biosynthesis in algae with complex plastids
Bacterial Isothiocyanate Biosynthesis by Rhodanese‐Catalyzed Sulfur Transfer onto Isonitriles
Synthesis of iron sulfur clusters as models for primordial life
Synthesis of iron sulfur clusters as models for primordial life
An algal enzyme required for biosynthesis of the most abundant marine carotenoids
Iron-sulfur cluster biosynthesis : : characterization of Escherichia coli cyay as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
The NSL complex is required for piRNA production from telomeric clusters
MondoA regulates gene expression in cholesterol biosynthesis-associated pathways required for zebrafish epiboly
Biosynthesis of iron-sulfur clusters and tetrapyrroles in microorganisms
Iron-sulfur clusters in chemistry and biology, Volume 2.. Biochemistry, biosynthesis and human diseases
Iron-sulfur clusters in chemistry and biology
The sulfur oxygenase reductase from Acidianus ambivalens : functional and structural characterization of a sulfur-disproportionating enzyme
Iron–Sulfur cluster biosynthesis in algae with complex plastids
Bacterial Isothiocyanate Biosynthesis by Rhodanese‐Catalyzed Sulfur Transfer onto Isonitriles
Synthesis of iron sulfur clusters as models for primordial life
Synthesis of iron sulfur clusters as models for primordial life
An algal enzyme required for biosynthesis of the most abundant marine carotenoids
Iron-sulfur cluster biosynthesis : : characterization of Escherichia coli cyay as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
The NSL complex is required for piRNA production from telomeric clusters
MondoA regulates gene expression in cholesterol biosynthesis-associated pathways required for zebrafish epiboly
Biosynthesis of iron-sulfur clusters and tetrapyrroles in microorganisms
Iron-sulfur clusters in chemistry and biology, Volume 2.. Biochemistry, biosynthesis and human diseases
Iron-sulfur clusters in chemistry and biology
The sulfur oxygenase reductase from Acidianus ambivalens : functional and structural characterization of a sulfur-disproportionating enzyme
Iron–Sulfur cluster biosynthesis in algae with complex plastids
Bacterial Isothiocyanate Biosynthesis by Rhodanese‐Catalyzed Sulfur Transfer onto Isonitriles
Synthesis of iron sulfur clusters as models for primordial life
Synthesis of iron sulfur clusters as models for primordial life
An algal enzyme required for biosynthesis of the most abundant marine carotenoids
Iron-sulfur cluster biosynthesis : : characterization of Escherichia coli cyay as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
The NSL complex is required for piRNA production from telomeric clusters