Decomposition of hydrogen peroxide by metmyoglobin: A cyclic formation of the ferryl intermediate |
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| Institution: | 1. College of Engineering and Technology, Southwest University, Chongqing 400715, China;2. College of Big Data, Yunnan Agricultural University, Kunming 650201, China;1. Ceramics and Biomaterials Research Group, Advanced Institute of Materials Science, Ton Duc Thang University, Ho Chi Minh City, Viet Nam;2. Faculty of Applied Sciences, Ton Duc Thang University, Ho Chi Minh City, Viet Nam;3. Faculty of Natural Sciences, Thu Dau Mot University, Binh Duong, Viet Nam;4. Faculty of Materials Science and Technology, University of Science, Viet Nam National University Ho Chi Minh City, 227 Nguyen Van Cu, District 5, Ho Chi Minh City, Viet Nam;5. Nhatrang Institute of Technology Research and Application, Vietnam Academy of Science and Techonoly, 02 Hung Vuong, Nha Trang, Khanh Hoa Province, Viet Nam;6. Simulation in Materials Science Research Group, Advanced Institute of Materials Science, Ton Duc Thang University, Ho Chi Minh City, Viet Nam;7. Key Laboratory of Photoelectric Detection Materials and Devices of Zhejiang Province, Ningbo 315211, PR China;8. Key Laboratory of Advanced Materials of Yunnan Province, School of Materials Science and Engineering, Kunming University of Science and Technology, Kunming 650093, China;1. VSB - Technical University of Ostrava, Faculty of Electrical Engineering and Computer Science, Department of Applied Mathematics, Czech Republic;2. Institute of Information Theory and Automation, Prague, Czech Republic;3. Department of Mathematical Science, Durham University, Durham, UK |
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| Abstract: | - 1.1. Metmyoglobin reacted with H2O2 to form ferryl-myoglobin, which reverted back spontaneously to the met-form.
- 2.2. Through this cyclic reaction of myoglobin between metMb(III) and ferryl-Mb(IV), we propose that H2O2, one of the potent oxidants in vivo, can be decomposed continuously in cardiac and skeletal muscle tissues in the absence of catalase and peroxidase.
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