Hemoprotein-based supramolecular assembling systems

Oohora, Koji; Hayashi, Takashi

doi:10.1016/j.cbpa.2014.02.014

Cited by 79 publications

(50 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…13C). Based on these observations, Hayashi and co-workers [9,119] developed a novel approach for assembling heme proteins to create supramolecular systems, such as a successive heme protein array with a length of 200-800 nm including 50-200 protein molecules [120,121]. Moreover, as reviewed recently by Hayashi [9,119], Ueno [122] and their co-workers, this strategy is useful for constructing hybrid materials with electrodes, nanoparticles or nanocups, generating novel biomaterials, biodevices and bioreactors with improved properties and functions.…”

Section: Cross-linking With Heme Propionate Group(s)mentioning

confidence: 92%

“…In natural heme proteins, the two propionate groups of heme usually form hydrogen-bonding interactions with the polypeptide chain and contribute to the heme stability [1][2][3][4][5][6][7][8][9][10][11]. Currently, there has been no discovery of a natural heme-protein cross-link involving the heme propionate group.…”

Section: Cross-linking With Heme Propionate Group(s)mentioning

confidence: 98%

“…For example, Cys-heme cross-link has recently been successfully used for design of functional cyt c-like oxidoreductases [147]. Therefore, as reviewed herein, the tremendous progresses make us confident that design of heme-protein cross-links, ideally, in combination with other strategies [1][2][3][4][5][6][7][8][9][10][11]80,[148][149][150][151][152], may be applied to construct advanced artificial heme proteins with functionalities comparable to or even beyond those of natural heme proteins.…”

Section: Summary and Perspectivementioning

confidence: 99%

“…1), to confer such diverse functions. This is attributed to the variety of interactions between the heme cofactor and the protein polypeptide chain, such as the coordination of heme iron by various axial ligands (His, Met, Cys, water, etc) and the hydrogen-bonding interactions in the heme distal pocket [1][2][3][4][5][6][7][8][9][10][11]. In addition to these interactions, post-translational modifications (PTMs) also play key roles in tuning the structure and function of heme proteins.…”

Section: Introductionmentioning

confidence: 98%

“…peroxidase and cytochrome P450, CYP450) to signaling (e.g. CO censor CooA) [1][2][3][4][5][6][7][8][9][10]. It is remarkable that heme proteins use the same heme cofactor, Fe-protoporphyrin IX (Fig.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

The broad diversity of heme-protein cross-links: An overview

Lin

2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

View full text Add to dashboard Cite

Section: Cross-linking With Heme Propionate Group(s)mentioning

confidence: 92%

Section: Cross-linking With Heme Propionate Group(s)mentioning

confidence: 98%

Section: Summary and Perspectivementioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The broad diversity of heme-protein cross-links: An overview

Lin

2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

View full text Add to dashboard Cite

Rational Design of Heterodimeric Protein using Domain Swapping for Myoglobin

Lin¹,

Nagao²,

Zhang³

et al. 2014

Angewandte Chemie

View full text Add to dashboard Cite

Protein design is a useful method to create novel artificial proteins. We developed a rational approach to design a heterodimeric protein using domain swapping for horse myoglobin (Mb). As confirmed by X-ray crystallographic analysis, a heterodimeric Mb with two different active sites was produced efficiently from two surface mutants of Mb, in which the charges of two amino acids involved in the dimer salt bridges were reversed in each mutant individually, with the active site of one mutant modified. This study shows that the method of constructing heterodimeric Mb with domain swapping is useful for designing artificial multi-heme proteins.

show abstract

Supramolecular Control over Split‐Luciferase Complementation

et al. 2016

View full text Add to dashboard Cite

Supramolecular split‐enzyme complementation restores enzymatic activity and allows for on–off switching. Split‐luciferase fragment pairs were provided with an N‐terminal FGG sequence and screened for complementation through host‐guest binding to cucurbit[8]uril (Q8). Split‐luciferase heterocomplex formation was induced in a Q8 concentration dependent manner, resulting in a 20‐fold upregulation of luciferase activity. Supramolecular split‐luciferase complementation was fully reversible, as revealed by using two types of Q8 inhibitors. Competition studies with the weak‐binding FGG peptide revealed a 300‐fold enhanced stability for the formation of the ternary heterocomplex compared to binding of two of the same fragments to Q8. Stochiometric binding by the potent inhibitor memantine could be used for repeated cycling of luciferase activation and deactivation in conjunction with Q8, providing a versatile module for in vitro supramolecular signaling networks.

show abstract

Hemoprotein-based supramolecular assembling systems

Cited by 79 publications

References 47 publications

The broad diversity of heme-protein cross-links: An overview

The broad diversity of heme-protein cross-links: An overview

Rational Design of Heterodimeric Protein using Domain Swapping for Myoglobin

Supramolecular Control over Split‐Luciferase Complementation

Contact Info

Product

Resources

About