Modification of Porous Protein Crystals in Development of Biohybrid Materials

Koshiyama, Tomomi; Kawaba, Naomi; Hikage, Tatsuo; Shirai, Masanobu; Miura, Yuki; Huang, Cheng Yuan; Tanaka, Kōichiro; Watanabe, Yoshihito; Ueno, Takafumi

doi:10.1021/bc9003052

Cited by 34 publications

(34 citation statements)

References 34 publications

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“…These crystals are able to capture and deposit metal ions and metal complexes within solvent channels when the crystals are soaked in the solutions containing the metal ions because the amino acid side chains responsible for coordinating the metal ions are periodically aligned on the surface of solvent channels of the crystal lattices 17–22. We have demonstrated the accumulation of functional molecules such as metal complexes and metal clusters into the solvent channels of porous myoglobin crystals by chemical conjugation and coordination interactions 23, 24. With respect to inorganic materials, it has been reported that protein crystals can serve as nanoreactors for the preparation of nanoparticles 25, 26.…”

Section: Characteristics Of the Copt‐nps Prepared In The Hewl Crystalmentioning

confidence: 98%

Porous Protein Crystals as Reaction Vessels for Controlling Magnetic Properties of Nanoparticles

Abe

Tsujimoto

Yoneda³

et al. 2012

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Section: Characteristics Of the Copt‐nps Prepared In The Hewl Crystalmentioning

confidence: 98%

Porous Protein Crystals as Reaction Vessels for Controlling Magnetic Properties of Nanoparticles

Abe

Tsujimoto

Yoneda³

et al. 2012

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“…Methyl viologen (MV) mediated the electron transfer between Zn porphyrin (ZnP, electron donor) and an oxo‐centered triruthenium cluster (Ru 3 O), electron acceptor) in the crystal. Remarkably, the Mb crystals form a channel structure with a diameter of 2–4 nm, which provides enough space for the accumulation of the functionalizing compounds . The applied crystal soaking method enabled the site‐specific fixation of Ru 3 O and the anisotropic diffusion of MV.…”

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

166

118

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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.

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“…The Mb crystals with space group P6 form several channel structures (diameter 2-4 nm), which provide enough space for accumulation of nanosized functional molecules as previously reported. [24] The Mb crystal spaces are available for site-specific fixation of Ru 3 O and anisotropic diffusion of MV. Moreover, fixation of zinc porphyrin units with a light-harvesting function in the Mb crystal is achieved by crystallization of zinc porphyrin substituted myoglobin (ZnMb).…”

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Post‐Crystal Engineering of Zinc‐Substituted Myoglobin to Construct a Long‐Lived Photoinduced Charge‐Separation System

et al. 2011

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Photoinduced electron transfer (ET) in native photosynthesis reactions is efficiently achieved by the accumulation of different types of redox cofactors within protein assemblies immobilized in cell membranes. [1][2][3] The precise arrangement of each cofactor in the molecular spaces enables them to retain the long-lived charge-separated state, which promotes multistep reactions in biological systems. To elucidate the mechanism of the biological ET reactions and to develop light energy conversion systems, artificial ET proteins have been constructed using de novo proteins, chemical modification of native cofactors, photocatalytic reaction centers engineered into protein assemblies, and design of synthetic metal complexes immobilized in protein-protein ET systems. [4][5][6][7][8][9][10][11][12] The reported systems have provided insights into control of ET rates in terms of the distance between donors and acceptors, hydrogen-bonding interactions, reorganization energy of cofactors, and other factors. [4][5][6][7][8][9][10][11][12] Control of the dense accumulation of the different redox cofactors observed in natural photosystems required to achieve long-lived charge-separated state has caused difficulties in efforts to duplicate this process using artificial protein systems in solution. [13] Thus, the design of novel protein frameworks that allow construction of a dense array of various cofactors is a worthwhile goal.Protein crystals can be regarded as excellent candidates for the development of artificial ET reaction systems because the crystal lattices are expected to allow different types of cofactors to be arranged in three-dimensional frameworks that mimic the native ET systems. ET reactions in single protein crystals have been investigated for the dependence of long-range ET on the structures and orientations of redox centers within proteins. [14][15][16] Gray et al. constructed photochemically-initiated protein-protein ET reactions in protein crystals containing zinc-substituted cytochrome c peroxidase or ruthenium-modified azurin. [14][15][16] Moreover, protein crystals provide nanosized spaces for the fixation of metal ions, metal complexes, and the diffusion of organic molecules. [17][18][19][20][21][22] For instance, accumulation of metal ions and metal complexes in a protein crystal lattice spaces was accomplished simply by soaking of the crystals in a solution containing their precursors. [17][18][19] Anisotropic diffusion of small molecules in hen egg-white lysozyme (HEWL) crystals has been investigated by experimental and simulation approaches. [21,22] The results suggest that these features are governed by steric repulsion and electrostatic interaction induced by amino acid residues located on the internal surface of the crystal lattices. Thus, if we can precisely arrange donor and acceptor molecules and mediators in protein crystals, it is expected that the novel three-dimensional framework will allow us to achieve a longlived charge-separated state.Herein, we construct an artificial long-lived ph...

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Modification of Porous Protein Crystals in Development of Biohybrid Materials

Cited by 34 publications

References 34 publications

Porous Protein Crystals as Reaction Vessels for Controlling Magnetic Properties of Nanoparticles

Porous Protein Crystals as Reaction Vessels for Controlling Magnetic Properties of Nanoparticles

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

Post‐Crystal Engineering of Zinc‐Substituted Myoglobin to Construct a Long‐Lived Photoinduced Charge‐Separation System

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