Analysis of ferrylHb radical reduction by L-tyrosine and its application to hemoglobin vesicles

Tomovasu Atoji; Hirotaka Yatami; Motonari Aihara; Eishun Tsuchida; Shinji Takeoka

Analysis of ferrylHb radical reduction by L-tyrosine and its application to hemoglobin vesicles

Tomovasu Atoji^*, Hirotaka Yatami, Motonari Aihara, Eishun Tsuchida, Shinji Takeoka

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to conference › Paper › peer-review

Abstract

We found that a mixed solution of methemoglobin (metHb) and L-tyrosine (L-Tyr) showed an effective H₂O₂ elimination ability by utilizing the peroxidase activity of metHb using L-Tyr as a substrate. The rapid radical disappearance and the appearance of metHb signal by L-Tyr addition were confirmed in the ESR measurement. In the mechanism, ferrylHb radicals are reduced to metHb by the electron donation from L-Tyr. From these results, stable H₂O₂ elimination by metHb/L-Tyr mixed solution would be due to the combination of peroxidase and pseudo-catalase activity of ferrylHb radicals. Furthermore, in the application to the Hb vesicles co-encapsulating metHb/L-Tyr, the 50 % metHb conversion from oxyHb in the vesicles was prolonged to 44 hr from 14hr of the Hb vesicles without metHb/L-Tyr.

Original language	English
Number of pages	1
Publication status	Published - 2006 Oct 19
Event	55th SPSJ Annual Meeting - Nagoya, Japan Duration: 2006 May 24 → 2006 May 26

Conference

Conference	55th SPSJ Annual Meeting
Country/Territory	Japan
City	Nagoya
Period	06/5/24 → 06/5/26

Keywords

FerrylHb radical
Hemoglobin vesicles
L-Tyr
Methb
Peroxidase activity

ASJC Scopus subject areas

Engineering(all)

Cite this

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title = "Analysis of ferrylHb radical reduction by L-tyrosine and its application to hemoglobin vesicles",

abstract = "We found that a mixed solution of methemoglobin (metHb) and L-tyrosine (L-Tyr) showed an effective H2O2 elimination ability by utilizing the peroxidase activity of metHb using L-Tyr as a substrate. The rapid radical disappearance and the appearance of metHb signal by L-Tyr addition were confirmed in the ESR measurement. In the mechanism, ferrylHb radicals are reduced to metHb by the electron donation from L-Tyr. From these results, stable H2O2 elimination by metHb/L-Tyr mixed solution would be due to the combination of peroxidase and pseudo-catalase activity of ferrylHb radicals. Furthermore, in the application to the Hb vesicles co-encapsulating metHb/L-Tyr, the 50 % metHb conversion from oxyHb in the vesicles was prolonged to 44 hr from 14hr of the Hb vesicles without metHb/L-Tyr.",

keywords = "FerrylHb radical, Hemoglobin vesicles, L-Tyr, Methb, Peroxidase activity",

author = "Tomovasu Atoji and Hirotaka Yatami and Motonari Aihara and Eishun Tsuchida and Shinji Takeoka",

year = "2006",

month = oct,

day = "19",

language = "English",

note = "55th SPSJ Annual Meeting ; Conference date: 24-05-2006 Through 26-05-2006",

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TY - CONF

T1 - Analysis of ferrylHb radical reduction by L-tyrosine and its application to hemoglobin vesicles

AU - Atoji, Tomovasu

AU - Yatami, Hirotaka

AU - Aihara, Motonari

AU - Tsuchida, Eishun

AU - Takeoka, Shinji

PY - 2006/10/19

Y1 - 2006/10/19

N2 - We found that a mixed solution of methemoglobin (metHb) and L-tyrosine (L-Tyr) showed an effective H2O2 elimination ability by utilizing the peroxidase activity of metHb using L-Tyr as a substrate. The rapid radical disappearance and the appearance of metHb signal by L-Tyr addition were confirmed in the ESR measurement. In the mechanism, ferrylHb radicals are reduced to metHb by the electron donation from L-Tyr. From these results, stable H2O2 elimination by metHb/L-Tyr mixed solution would be due to the combination of peroxidase and pseudo-catalase activity of ferrylHb radicals. Furthermore, in the application to the Hb vesicles co-encapsulating metHb/L-Tyr, the 50 % metHb conversion from oxyHb in the vesicles was prolonged to 44 hr from 14hr of the Hb vesicles without metHb/L-Tyr.

AB - We found that a mixed solution of methemoglobin (metHb) and L-tyrosine (L-Tyr) showed an effective H2O2 elimination ability by utilizing the peroxidase activity of metHb using L-Tyr as a substrate. The rapid radical disappearance and the appearance of metHb signal by L-Tyr addition were confirmed in the ESR measurement. In the mechanism, ferrylHb radicals are reduced to metHb by the electron donation from L-Tyr. From these results, stable H2O2 elimination by metHb/L-Tyr mixed solution would be due to the combination of peroxidase and pseudo-catalase activity of ferrylHb radicals. Furthermore, in the application to the Hb vesicles co-encapsulating metHb/L-Tyr, the 50 % metHb conversion from oxyHb in the vesicles was prolonged to 44 hr from 14hr of the Hb vesicles without metHb/L-Tyr.

KW - FerrylHb radical

KW - Hemoglobin vesicles

KW - L-Tyr

KW - Methb

KW - Peroxidase activity

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M3 - Paper

AN - SCOPUS:33749850657

T2 - 55th SPSJ Annual Meeting

Y2 - 24 May 2006 through 26 May 2006

ER -

Analysis of ferrylHb radical reduction by L-tyrosine and its application to hemoglobin vesicles

Abstract

Conference

Keywords

ASJC Scopus subject areas

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