Preparation and O2 binding study of myoglobin having a cobalt porphycene

Takashi Matsuo; Takashi Tsuruta; Keiko Maehara; Hideaki Sato; Yoshio Hisaeda; Takashi Hayashi

doi:10.1021/ic0513639

Preparation and O₂ binding study of myoglobin having a cobalt porphycene

Takashi Matsuo, Takashi Tsuruta, Keiko Maehara, Hideaki Sato, Yoshio Hisaeda, Takashi Hayashi

Research output: Contribution to journal › Article › peer-review

40 Citations (Scopus)

Abstract

Sperm whale myoglobin, an oxygen-storage hemoprotein, was reconstituted with 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl) porphycenatocobalt(II) in order to investigate the reactivities of a cobalt porphycene in a protein matrix. Similar to the previously reported finding for the myoglobin with the iron porphycene, the reconstituted myoglobin with the cobalt porphycene was also found to have an O₂ affinity 2 orders of magnitude greater than that of the myoglobin possessing cobalt protoporphyrin IX. The EPR spectra of the deoxy and oxy myoglobins having the cobalt porphycene at 77 K also have features similar to those of the myoglobin with cobalt protoporphyrin IX. These spectra suggest that the porphycene cobalt in the deoxy form is coordinated by one nitrogenous ligand postulated to be the imidazole ring of His93, and that the bond configuration of Co^II-O₂ is regarded as the Co^III-O₂^•- species.

Original language	English
Pages (from-to)	9391-9396
Number of pages	6
Journal	Inorganic chemistry
Volume	44
Issue number	25
DOIs	https://doi.org/10.1021/ic0513639
Publication status	Published - Dec 12 2005

All Science Journal Classification (ASJC) codes

Physical and Theoretical Chemistry
Inorganic Chemistry

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title = "Preparation and O2 binding study of myoglobin having a cobalt porphycene",

abstract = "Sperm whale myoglobin, an oxygen-storage hemoprotein, was reconstituted with 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl) porphycenatocobalt(II) in order to investigate the reactivities of a cobalt porphycene in a protein matrix. Similar to the previously reported finding for the myoglobin with the iron porphycene, the reconstituted myoglobin with the cobalt porphycene was also found to have an O2 affinity 2 orders of magnitude greater than that of the myoglobin possessing cobalt protoporphyrin IX. The EPR spectra of the deoxy and oxy myoglobins having the cobalt porphycene at 77 K also have features similar to those of the myoglobin with cobalt protoporphyrin IX. These spectra suggest that the porphycene cobalt in the deoxy form is coordinated by one nitrogenous ligand postulated to be the imidazole ring of His93, and that the bond configuration of CoII-O2 is regarded as the CoIII-O2•- species.",

author = "Takashi Matsuo and Takashi Tsuruta and Keiko Maehara and Hideaki Sato and Yoshio Hisaeda and Takashi Hayashi",

year = "2005",

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doi = "10.1021/ic0513639",

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T1 - Preparation and O2 binding study of myoglobin having a cobalt porphycene

AU - Matsuo, Takashi

AU - Tsuruta, Takashi

AU - Maehara, Keiko

AU - Sato, Hideaki

AU - Hisaeda, Yoshio

AU - Hayashi, Takashi

PY - 2005/12/12

Y1 - 2005/12/12

N2 - Sperm whale myoglobin, an oxygen-storage hemoprotein, was reconstituted with 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl) porphycenatocobalt(II) in order to investigate the reactivities of a cobalt porphycene in a protein matrix. Similar to the previously reported finding for the myoglobin with the iron porphycene, the reconstituted myoglobin with the cobalt porphycene was also found to have an O2 affinity 2 orders of magnitude greater than that of the myoglobin possessing cobalt protoporphyrin IX. The EPR spectra of the deoxy and oxy myoglobins having the cobalt porphycene at 77 K also have features similar to those of the myoglobin with cobalt protoporphyrin IX. These spectra suggest that the porphycene cobalt in the deoxy form is coordinated by one nitrogenous ligand postulated to be the imidazole ring of His93, and that the bond configuration of CoII-O2 is regarded as the CoIII-O2•- species.

AB - Sperm whale myoglobin, an oxygen-storage hemoprotein, was reconstituted with 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl) porphycenatocobalt(II) in order to investigate the reactivities of a cobalt porphycene in a protein matrix. Similar to the previously reported finding for the myoglobin with the iron porphycene, the reconstituted myoglobin with the cobalt porphycene was also found to have an O2 affinity 2 orders of magnitude greater than that of the myoglobin possessing cobalt protoporphyrin IX. The EPR spectra of the deoxy and oxy myoglobins having the cobalt porphycene at 77 K also have features similar to those of the myoglobin with cobalt protoporphyrin IX. These spectra suggest that the porphycene cobalt in the deoxy form is coordinated by one nitrogenous ligand postulated to be the imidazole ring of His93, and that the bond configuration of CoII-O2 is regarded as the CoIII-O2•- species.

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JO - Inorganic chemistry

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IS - 25

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Preparation and O₂ binding study of myoglobin having a cobalt porphycene

Abstract

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