Supramolecular Linear Assemblies of Cytochrome b 562 Immobilized on a Gold Electrode

Kakikura, Yasuaki; Onoda, Akira; Kubo, Emi; Kitagishi, Hiroaki; Uematsu, Taro; Kuwabata, Susumu; Hayashi, Takashi

doi:10.1007/s10904-012-9737-1

Cited by 10 publications

(8 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S6 and S7 † ). 27 , 31 – 33 We confirm the anchoring of Pc CDH F+H– onto heme/Au by visualizing the process of protein reconstitution using HS-AFM (Fig. S8 † ).…”

Section: Resultsmentioning

confidence: 55%

Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…S6 and S7 † ). 27 , 31 – 33 We confirm the anchoring of Pc CDH F+H– onto heme/Au by visualizing the process of protein reconstitution using HS-AFM (Fig. S8 † ).…”

Section: Resultsmentioning

confidence: 55%

Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…Hemoproteins tightly bind a heme (iron protoporphyrin IX) as a cofactor by coordination and noncovalent interactions, thereby enabling the desired supramolecular protein–polymer interaction and immobilization onto a metal surface via a heme–heme pocket interaction. Our group has reported several different types of hemoprotein assemblies and immobilization of the assemblies on an electrode or a metal colloid by a noncovalent heme–heme pocket interaction. These outcomes further encouraged us to design and prepare protein‐based hybrid biomaterials constructed from a hemoprotein and a synthetic polymer by taking advantage of the supramolecular cofactor–protein interaction.…”

Section: Figurementioning

confidence: 99%

Oxygen‐binding Protein Fiber and Microgel: Supramolecular Myoglobin–Poly(acrylate) Conjugates

Ono

Hisaoka

Onoda

et al. 2016

Chemistry An Asian Journal

Self Cite

View full text Add to dashboard Cite

A supramolecular conjugate of myoglobin (Mb) and water-soluble poly(acrylate), (PA5k and PA25k , where 5k and 25k represent the molecular weight of the polymers, respectively), is constructed on the basis of a noncovalent heme-heme pocket interaction. The modified heme with an amino group linked to the terminus of one of the heme-propionates is coupled to the side-chain carboxyl groups of poly(acrylate) activated by N-hydroxysuccinimide. The ratios of the heme-modified monomer unit and the unmodified monomer unit (m:n) in the polymer chains of Heme-PA5k and Heme-PA25k were determined to be 4.5:95.5 and 3.1:96.9, respectively. Subsequent addition of apoMb to the conjugated polymers provides Mb-connected fibrous nanostructures confirmed by atomic force microscopy. A mixture of the heme-modified polymer and dimeric apomyoglobin as a cross-linker forms a microgel in which the reconstituted myoglobin retains its native exogenous ligand binding activity.

show abstract

“…Here, we highlight recent works focused on the construction of fibrous, branched and cross-linked hemoprotein polymers and hybrid conjugates with other attractive materials such as electrodes and nanoparticles. [50][51][52][53][54][55][56][57][58][59] From the present article, it is proposed that appropriate modification of a cofactor and hemoprotein by synthetic and mutagenesis techniques will provide a variety of hemoprotein self-assembly structures with useful protein functions (example iv in Scheme 1).…”

Section: Takashi Hayashimentioning

confidence: 99%

Supramolecular assembling systems formed by heme–heme pocket interactions in hemoproteins

2012

Self Cite

View full text Add to dashboard Cite

A native protein in a biological system spontaneously produces large and elegant assemblies via self-assembly or assembly with various biomolecules which provide non-covalent interactions. In this context, the protein plays a key role in construction of a unique supramolecular structure operating as a functional system. Our group has recently highlighted the structure and function of hemoproteins reconstituted with artificially created heme analogs. The heme molecule is a replaceable cofactor of several hemoproteins. Here, we focus on the successive supramolecular protein assemblies driven by heme-heme pocket interactions to afford various examples of protein fibers, networks and three-dimensional clusters in which an artificial heme moiety is introduced onto the surface of a hemoprotein via covalent linkage and the native heme cofactor is removed from the heme pocket. This strategy is found to be useful for constructing hybrid materials with an electrode or with nanoparticles. The new systems described herein are expected to lead to the generation of various biomaterials with functions and characteristic physicochemical properties similar to those of hemoproteins.

show abstract

Supramolecular Linear Assemblies of Cytochrome b 562 Immobilized on a Gold Electrode

Cited by 10 publications

References 48 publications

Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

Oxygen‐binding Protein Fiber and Microgel: Supramolecular Myoglobin–Poly(acrylate) Conjugates

Supramolecular assembling systems formed by heme–heme pocket interactions in hemoproteins

Contact Info

Product

Resources

About