Porous Protein Crystals as Catalytic Vessels for Organometallic Complexes

Tabe, Hiroyasu; Abe, Satoshi; Hikage, Tatsuo; Kitagawa, Susumu; Ueno, Takafumi

doi:10.1002/asia.201301347

Cited by 52 publications

(60 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enantiomeric excesses were different from those previously measured with the βLG biohybrids and, quite surprisingly, the mixture of HEWL and Ir(Cp*) afforded preferentially the S enantiomer of α‐(trifluoromethyl)benzyl alcohol, whereas the mixtures of HEWL and the Ru complexes gave the R isomer as before. The rather poor selectivity of the HEWL + Ru(benz) mixture is in line with previously reported results for other acetophenone derivatives …”

Section: Resultssupporting

confidence: 92%

“…It has been recently shown that association of Ru(benz) and cross‐linked crystals of HEWL catalyse the TH of acetophenone derivatives with variable selectivity . Thus, as a preliminary screening, we examined the ability of crude mixtures of HEWL and hydrolysed M(arene) complexes (M = Ru, arene = benz or p ‐cym; M = Rh or Ir, L = Cp*) at molar ratio 1:1 to catalyse the ATH of TFACP.…”

Section: Resultsmentioning

confidence: 99%

“…A more serendipitous approach is to make use of the latent coordination ability of proteins to bind catalytically active metal centres. This approach has been employed with variable success in a small set of protein scaffolds (albumin, apoferritin, lysozyme and streptavidin) and transition metal complexes (Os, Pd, Rh, Mn, Fe, Ru and V). The best results in terms of enantioselectivity were obtained with albumin– and streptavidin–osmium tetroxide hybrids, which catalysed the cis ‐dihydroxylation of α‐methylstyrene with up to 68[13a] and 95 %[16a] ee , respectively.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Proteins as Macromolecular Ligands for Metal‐Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium

2018

View full text Add to dashboard Cite

Biohybrid catalysts resulting from the dative anchoring of half-sandwich organometallic complexes [M(arene)-(H 2 O) x (Cl) y ] n+ (M = Ru II , arene = η 6 -benzene, p-cymene or mesitylene; M = Ir III , Rh III , arene = η 5 -Cp*; x = 1-3, y = 0-2, n = 0-2) to bovine beta-lactoglobulin ( LG) or hen egg white lysozyme showed unprecedented behaviour. These constructs were shown to catalyse the asymmetric transfer hydrogenation of aryl ketones in water with sodium formate as hydrogen donor at a much faster rate than the complexes alone. Full conversion of the benchmark substrate 2,2,2-trifluoroacetophenone was reached with an ee of 86 % for the most selective biohybrid. Surprisingly, even the crude biohybrid gave a good ee despite [a] 1385 terns of the most prominent 15+ ion of LG-A and LG-A + Ru(benz) were compared (Figure 3). Full PaperFigure 3. Isotopic distribution of the 15+ ion for LG-A (A) and LG-A + Ru(benz) (B) with experimental (top) and calculated (bottom) patterns. Such values can certainly be attributed to complexation ofLG-A with one and two [Ru(benz)] 2+ units In addition, according to the aforementioned values, good agreement was also obtained with theoretical masses: 18529.3882 g mol -1 (5th isotope; 5 ppm) and 18707.3452 g mol -1 (5th isotope; 3 ppm) forLG-A + one Ru(benz) andLG-A + two [Ru(benz)], respectively. Assuming that all species exhibit a similar ESI response factor,

show abstract

Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Proteins as Macromolecular Ligands for Metal‐Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium

2018

View full text Add to dashboard Cite

show abstract

“…Most frequently investigated, as molecular templates for the synthesis of artificial protein crystal assemblies, are hen egg white lysozyme (HEWL) crystals. Tabe and co‐workers investigated cross‐linked HEWL crystals for their application as catalytic reaction vessels by accumulating organometallic complexes in the solvent channels of the crystals (Figure ) . The cross‐linked crystals were soaked in a buffer solution containing [Ru(benzene)Cl 2 ] 2 complexes for the preparation of Ru(benzene)‐CL‐HEWL composites.…”

Section: Chemoenzymatic Cascade Reactionsmentioning

confidence: 99%

Overcoming the Incompatibility Challenge in Chemoenzymatic and Multi‐Catalytic Cascade Reactions

Schmidt

Castiglione

Kourist

2017

Chemistry A European J

171

118

View full text Add to dashboard Cite

Multi-catalytic cascade reactions bear a great potential to minimize downstream and purification steps, leading to a drastic reduction of the produced waste. In many examples, the compatibility of chemo- and biocatalytic steps could be easily achieved. Problems associated with the incompatibility of the catalysts and their reactions, however, are very frequent. Cascade-like reactions can hardly occur in this way. One possible solution to combine, in principle, incompatible chemo- and biocatalytic reactions is the defined control of the microenvironment by compartmentalization or scaffolding. Current methods for the control of the microenvironment of biocatalysts go far beyond classical enzyme immobilization and are thus believed to be very promising tools to overcome incompatibility issues and to facilitate the synthetic application of cascade reactions. In this Minireview, we will summarize recent synthetic examples of (chemo)enzymatic cascade reactions and outline promising methods for their spatial control either by using bio-derived or synthetic systems.

show abstract

“…43,44 Postengineering of CLPCs has recently been performed to convert solvent channels into nanovessels for preparation of metal particles or immobilization of organometallic catalysts. 20,41,42 The success of these efforts indicates that protein crystals have further potential to provide new structures and improve the reactivity of CORMs when used as extracellular scaffolds for supporting CO-releasing molecules.…”

Section: ■ Introductionmentioning

confidence: 98%

Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold

et al. 2014

Self Cite

View full text Add to dashboard Cite

Protein crystals generally are stable solid protein assemblies. Certain protein crystals are suitable for use as nanovessels for immobilizing metal complexes. Here we report the preparation of ruthenium carbonyl-incorporated cross-linked hen egg white lysozyme crystals (Ru·CL-HEWL). Ru·CL-HEWL retains a Ru carbonyl moiety that can release CO, although a composite of Ru carbonyl-HEWL dissolved in buffer solution (Ru·HEWL) does not release CO. We found that treatment of cells with Ru·CL-HEWL significantly increased nuclear factor kappa B (NF-κB) activity as a cellular response to CO. These results demonstrate that Ru·CL-HEWL has potential for use as an artificial extracellular scaffold suitable for transport and release of a gas molecule.

show abstract

Porous Protein Crystals as Catalytic Vessels for Organometallic Complexes

Cited by 52 publications

References 67 publications

Proteins as Macromolecular Ligands for Metal‐Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium

Proteins as Macromolecular Ligands for Metal‐Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium

Overcoming the Incompatibility Challenge in Chemoenzymatic and Multi‐Catalytic Cascade Reactions

Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold

Contact Info

Product

Resources

About