Blue Myoglobin Reconstituted with an Iron Porphycene Shows Extremely High Oxygen Affinity-Reference-Cited by-同舟云学术

Blue Myoglobin Reconstituted with an Iron Porphycene Shows Extremely High Oxygen Affinity

Published:2002-08-28 Issue:38 Volume:124 Page:11226-11227
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hayashi Takashi¹,Dejima Hirohisa¹,Matsuo Takashi¹,Sato Hideaki¹,Murata Dai¹,Hisaeda Yoshio¹

Affiliation:

1. Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, and PRESTO in Japan Science and Technology Corporation, Fukuoka 812-8581, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0265052

Reference30 articles.

1. Mechanisms of Ligand Recognition in Myoglobin

2. Controlling Ligand Binding in Myoglobin by Mutagenesis

3. Engineering Ascaris hemoglobin oxygen affinity in sperm whale myoglobin: role of tyrosine B10

4. Raven, E. L.; Mauk, A. G. InAdvances in Inorganic Chemistry; Sykes, A. G., Mauk, G., Eds.; Academic Press: San Diego, 2001; Vol. 51, pp 1−51.

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