Novel Chemical Modification of Myoglobin by an Alcohol-Responsive Phenylboronic Acid Function

Nagasaki, Takeshi; Kimura, Onari; Hamachi, Itaru; Shinkai, Seiji

doi:10.1246/cl.1994.1945

Cited by 2 publications

(1 citation statement)

References 5 publications

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“…Although, in nature, the essential role of Mb is oxygen storage, semiartificial myoglobins possessing nonnatural functions and/or artificial molecular binding sites have been prepared by a reconstitutional method that involves incorporation of an artificial heme with multiple functional groups into apomyoglobin (apo‐Mb) 2–4. For example, Hamachi and co‐workers have synthesized artificial heme molecules modified with various functional chromophores, such as catenane,2a–c a ruthenium–tris(bipyridine) complex,2d–g iminodiacetic acid,2h riboflavin,2i C 60 ,2j lipids,2k β‐cyclodextrin,2l–n and boronic acids 2o–q. By using these synthetic heme molecules, they achieved the functional conversion and regulation of Mb.…”

Section: Introductionmentioning

confidence: 99%

De Novo Design, Synthesis, and Function of Semiartificial Myoglobin Conjugated with Coiled‐Coil Two‐α‐Helix Peptides

Sakamoto

Ito

Kudo

2004

Chemistry A European J

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The introduction of a flavin chromophore on the myoglobin (Mb) surface and an effective electron-transfer (ET) reaction through the flavin were successfully achieved by utilizing the self-assembly of heterostranded coiled-coil peptides. We have prepared a semiartificial Mb, named Mb-1alphaK, in which an amphiphilic and cationic alpha-helix peptide is conjugated at the heme propionate (Heme-1alphaK). Heme-1alphaK has a covalently bound iron-protoporphyrin IX (heme) at the N terminus of a 1alphaK peptide sequence. This sequence was designed to form a heterostranded coiled-coil in the presence of a counterpart amphiphilic and anionic 1alphaE peptide sequence in a parallel orientation. Two peptides, Fla(1)-1alphaE and Fla(31)-1alphaE, both incorporating a 10-methylisoalloxazine moiety as an artificial flavin molecule, were also prepared (Fla=2-[7-(10-methyl)isoalloxazinyl]-2-oxoethyl). Heme-1alphaK was successfully inserted into apomyoglobin to give Mb-1alphaK. Mb-1alphaK recognized the flavin-modified peptides and a two-alpha-helix structure was formed. In addition, an efficient ET from reduced nicotinamide adenine dinucleotide to the heme center through the flavin unit was observed. The ET rate was faster in the presence of Fla(1)-1alphaE than in the presence of Fla(31)-1alphaE or the equivalent molecule that has no peptide chain. These results demonstrate that the introduction of a functional chromophore on the Mb surface can be achieved by using specific peptide-peptide interactions. Moreover, the dependence of the ET rate on the position of the flavin indicated that the distance between the heme active site and the flavin chromophore was regulated by the three-dimensional structure of the designed polypeptide.

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Section: Introductionmentioning

confidence: 99%

De Novo Design, Synthesis, and Function of Semiartificial Myoglobin Conjugated with Coiled‐Coil Two‐α‐Helix Peptides

Sakamoto

Ito

Kudo

2004

Chemistry A European J

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Design and Synthesis of Sugar‐Responsive Semiartificial Myoglobin Triggered by Modulation of Apoprotein–Cofactor Interactions

Hamachi

Tajiri

Nagase

et al. 1997

Chemistry A European J

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Phenylboronic acid groups as sugar recognition sites were successfully introduced into native myoglobin by a cofactor-reconstitution method. Spectrophotometric pH titration demonstrated the sugar-induced pK, shift of the H,O coordinated to the heme center of the semisynthetic myoglobin bearing phenylboronic acids (met-Mb(PhBOH),). By means of circular dichroism (CD) and paramagnetic 'H NMR spectroscopies, it was provcn that sugars that were bound to phenylboronic acid sites induced the rearrangement of the heme crevice to reinforce the heme cofactor-apoprotein interactions. The structural changes that were induced by the binding o f sugars subsequently enhanced the dioxygen storage activity of Mb(PhBOH), . Such sugarinduced structural and functional changes did not occur for other modified Mbs that

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Novel Chemical Modification of Myoglobin by an Alcohol-Responsive Phenylboronic Acid Function

Cited by 2 publications

References 5 publications

De Novo Design, Synthesis, and Function of Semiartificial Myoglobin Conjugated with Coiled‐Coil Two‐α‐Helix Peptides

De Novo Design, Synthesis, and Function of Semiartificial Myoglobin Conjugated with Coiled‐Coil Two‐α‐Helix Peptides

Design and Synthesis of Sugar‐Responsive Semiartificial Myoglobin Triggered by Modulation of Apoprotein–Cofactor Interactions

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