A De Novo Designed Trimeric Metalloprotein as a Ni<sub>p</sub> Model of the Acetyl-CoA Synthase
We present a Ni<sub>p</sub> site model of acetyl coenzyme-A synthase (ACS) within a de novo-designed trimer peptide that self-assembles to produce a homoleptic Ni(Cys)<sub>3</sub> binding motif. Spectroscopic and kinetic studies of ligand binding demonstrate that Ni binding s...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-06-01
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| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/24/12/10317 |
| Summary: | We present a Ni<sub>p</sub> site model of acetyl coenzyme-A synthase (ACS) within a de novo-designed trimer peptide that self-assembles to produce a homoleptic Ni(Cys)<sub>3</sub> binding motif. Spectroscopic and kinetic studies of ligand binding demonstrate that Ni binding stabilizes the peptide assembly and produces a terminal Ni<sup>I</sup>-CO complex. When the CO-bound state is reacted with a methyl donor, a new species is quickly produced with new spectral features. While the metal-bound CO is albeit unactivated, the presence of the methyl donor produces an activated metal-CO complex. Selective outer sphere steric modifications demonstrate that the physical properties of the ligand-bound states are altered differently depending on the location of the steric modification above or below the Ni site. |
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| ISSN: | 1661-6596 1422-0067 |