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Capture of carbon monoxide using a heme protein model: from biomimetic chemistry of heme proteins to physiological and therapeutic applications

Polymer Journal volume 54, pages 465–472 (2022)Cite this article

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Abstract

Hemoglobin (Hb) and myoglobin (Mb) are heme proteins that capture and transport molecular oxygen (O2) in living organisms. Although mimicking the O2-binding function of Hb and Mb using synthetic iron-porphyrin has been extensively studied for over 40 years, mimicking the function of Hb/Mb in vivo or 100% aqueous solutions has been minimally studied. Hence, a supramolecular complex termed “hemoCD1” was constructed as the aqueous synthetic Hb/Mb model using a 1:1 inclusion complex of 5,10,15,20-tetrakis(4-sulfonatophenyl)porphinatoiron(II) (FeIITPPS) with a per-O-methylated β-cyclodextrin dimer with a pyridine linker (Py3CD). Selective carbon monoxide (CO) depletion in vivo is beneficial for studying the physiological roles of endogenous CO as a gaseous signal messenger. HemoCD1 reversibly binds O2 and CO in aqueous solution at ambient temperature. Hence, hemoCD1 was used as a selective CO scavenger in vivo due to its extremely high binding affinity to CO. In addition, hemoCD1 was utilized to quantify the accumulation of endogenous and exogenous CO in organs/tissues. Finally, hemoCD1 was employed as an antidote for CO poisoning in animals. Thus, recent developments in hemoCD1 have revealed that the aqueous biomimetic heme protein model has significant physiological and therapeutic application potential.

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Acknowledgements

This work was financially supported by JSPS KAKENHI Grant Numbers 20H02871, 20H04540, 19K22972, and 18KK0156, the MEXT-Supported Program for the Strategic Research Foundation at Private Universities (2015–2019), the Takeda Science Foundation, the NOVARTIS Foundation (Japan) for the Promotion of Science, the Suntory Foundation for Life Sciences, and the JGC-S Scholarship Foundation.

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  1. Department of Molecular Chemistry and Biochemistry, Faculty of Science and Engineering, Doshisha University, Kyotanabe-city, Kyoto, 610-0321, Japan

    Hiroaki Kitagishi & Qiyue Mao

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Correspondence to Hiroaki Kitagishi.

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Kitagishi, H., Mao, Q. Capture of carbon monoxide using a heme protein model: from biomimetic chemistry of heme proteins to physiological and therapeutic applications. Polym J 54, 465–472 (2022). https://doi.org/10.1038/s41428-021-00591-y

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