Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity.

Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Research Abstract Details 

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Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Abstract Text:

Takashi Hayashi,Hirohisa Dejima,Takashi Matsuo,Hideaki Sato,Dai Murata,Yoshio Hisaeda,

Myoglobin will be a good scaffold for engineering a function into proteins. To modulate the physiological function of myoglobin, almost all approaches have been demonstrated by site-directed mutagenesis, however, there are few studies which show a significant improvement in the function. In contrast, we focused on the replacement of heme in the protein with an artificial prosthetic group. Recently, we prepared a novel myoglobin reconstituted with an iron porphycene as a structural isomer of mesoheme. The bluish colored reconstituted myoglobin is relatively stable and the deoxymyoglobin reversibly binds ligands. Interestingly, the O2 affinity of the reconstituted myoglobin, 1.1 x 109 M-1, is a significant 1,400-fold higher than that of the native myoglobin. Furthermore, the unfavorable autoxidation kinetics show 7-fold decrease in rate for the reconstituted myoglobin relative to the native myoglobin, indicating the stable oxy-form against autoxidation. The net results come from the slow dissociation of the O2 ligand in the reconstituted myoglobin, koff = 0.11 s-1, because of the formation of strong hydrogen bond between His64 and negatively charged dioxygen. The present study indicates that the replacement of native heme with an artificially created prosthetic group will give us a unique function into a hemoprotein.

Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Publishing Authors By Initials

T Hayashi,H Dejima,T Matsuo,H Sato,D Murata,Y Hisaeda,

For similar heterocyclic compounds: heterocyclic compounds, 1-ring: azoles: pyrroles: tetrapyrroles: porphyrins research abstracts see: heterocyclic compounds: heterocyclic compounds, 1-ring: azoles: pyrroles: tetrapyrroles: porphyrins research

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Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Chemical Society

VOLUME: 124

Page Numbers: 11226-7

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 25

MONTH: Sep

YEAR: 2002

Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Keywords Mesh Terms:

KEYWORDS: Porphyrins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. Information

Substance Name: Oxygen

Registry Number: 7782-44-7

Grant and Affiliation Information for Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity.

AFFILIATION: Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, and PRESTO in Japan Science and Technology Corporation, Fukuoka 812-8581, Japan. thayatcm@mbox.nc.kyushu-u.ac.jp

Country: United States

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MEDLINETA: J Am Chem Soc

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