1. Characterization of the iron-sulfur clusters in the nitrogenase-like reductase CfbC/D required for coenzyme F 430 biosynthesis.
- Author
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Vazquez Ramos J, Kulka-Peschke CJ, Bechtel DF, Zebger I, Pierik AJ, and Layer G
- Subjects
- Oxidoreductases metabolism, Oxidoreductases genetics, Oxidoreductases chemistry, Nitrogenase metabolism, Nitrogenase chemistry, Nitrogenase genetics, Archaeal Proteins metabolism, Archaeal Proteins genetics, Archaeal Proteins chemistry, Cysteine metabolism, Sulfur metabolism, Sulfur chemistry, Metalloporphyrins, Iron-Sulfur Proteins metabolism, Iron-Sulfur Proteins genetics, Iron-Sulfur Proteins chemistry
- Abstract
Coenzyme F
430 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., (© 2024 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)- Published
- 2024
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