Dataset Information

Designed Syntheses of Three {Ni₆PW₉}-Based Polyoxometalates, from Isolated Cluster to Cluster-Organic Helical Chain.

ABSTRACT: Three new hexa-Ni-substituted Keggin-type polyoxometalates (POMs), [Ni₆(OH)₃- (DACH)₃(H₂O)₆(PW₉O₃₄)]·31H₂O (1), [Ni(DACH)₂][Ni₆(OH)₃(DACH)₃(HMIP)₂(H₂O)₂(PW₉O₃₄)]·56 H₂O (2), and [Ni(DACH)₂][Ni₆(OH)₃(DACH)₂(AP)(H₂O)₅(PW₉O₃₄)]·2H₂O (3) (DACH = 1,2-Diami- nocyclohexane, MIP = 5-Methylisophthalate, AP = Adipate) were successfully made in the presence of DACH under hydrothermal conditions. 1 is an isolated hexa-Ni-substituted Keggin unit decorated by DACH. In order to further construct POM cluster-organic frameworks (POMCOFs) on the basis of 1, by analyzing the steric hindrances and orientations of the POM units, the rigid HMIP and flexible AP ligands were successively incorporated, and another anionic monomeric POM 2 and the new 1D POM cluster organic chain (POMCOC) 3 were obtained. HMIP ligand still acts as a decorating group on the Ni₆ core of 2 but results in the different spatial arrangement of the {Ni₆PW₉} units. AP ligands in 3 successfully bridge adjacent isolated POM cluster units to 1D POMCOC with left-hand helices. The AP in 3 is the longest aliphatic carboxylic acid ligand in POMs, and the 1D POM cluster-AP helical chain represents the first 1D POMCOC with a helical feature.

SUBMITTER: Chen CA

PROVIDER: S-EPMC9268654 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Similar Datasets

Project description:The primary and secondary coordination spheres of metal binding sites in metalloproteins have been investigated extensively, leading to the creation of high-performing functional metalloproteins; however, the impact of the overall structure of the protein scaffold on the unique properties of metalloproteins has rarely been studied. A primary example is the binuclear CuA center, an electron transfer cupredoxin domain of photosynthetic and respiratory complexes and, recently, a protein coregulated with particulate methane and ammonia monooxygenases. The redox potential, Cu-Cu spectroscopic features, and a valence delocalized state of CuA are difficult to reproduce in synthetic models, and every artificial protein CuA center to-date has used a modified cupredoxin. Here, we present a fully functional CuA center designed in a structurally nonhomologous protein, cytochrome c peroxidase (CcP), by only two mutations (CuACcP). We demonstrate with UV-visible absorption, resonance Raman, and magnetic circular dichroism spectroscopy that CuACcP is valence delocalized. Continuous wave and pulsed (HYSCORE) X-band EPR show it has a highly compact gz area and small Az hyperfine principal value with g and A tensors that resemble axially perturbed CuA. Stopped-flow kinetics found that CuA formation proceeds through a single T2Cu intermediate. The reduction potential of CuACcP is comparable to native CuA and can transfer electrons to a physiological redox partner. We built a structural model of the designed Cu binding site from extended X-ray absorption fine structure spectroscopy and validated it by mutation of coordinating Cys and His residues, revealing that a triad of residues (R48C, W51C, and His52) rigidly arranged on one α-helix is responsible for chelating the first Cu(II) and that His175 stabilizes the binuclear complex by rearrangement of the CcP heme-coordinating helix. This design is a demonstration that a highly conserved protein fold is not uniquely necessary to induce certain characteristic physical and chemical properties in a metal redox center.

Dataset Information

Designed Syntheses of Three {Ni₆PW₉}-Based Polyoxometalates, from Isolated Cluster to Cluster-Organic Helical Chain.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Designed Syntheses of Three {Ni6PW9}-Based Polyoxometalates, from Isolated Cluster to Cluster-Organic Helical Chain.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Designed Syntheses of Three {Ni₆PW₉}-Based Polyoxometalates, from Isolated Cluster to Cluster-Organic Helical Chain.