Literature DB >> 8432378

Decomposition of hydrogen peroxide by metmyoglobin: a cyclic formation of the ferryl intermediate.

G Tajima1, K Shikama.   

Abstract

1. Metmyoglobin reacted with H2O2 to form ferryl-myoglobin, which reverted back spontaneously to the met-form. 2. Through this cyclic reaction of myoglobin between metMb(III) and ferryl-Mb(IV), we proposed 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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Year:  1993        PMID: 8432378     DOI: 10.1016/0020-711x(93)90495-z

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  2 in total

1.  Intracellular imaging of metmyoglobin and oxygen using new dual purpose probe EYFP-Myoglobin-mCherry.

Authors:  Rozhin Penjweini; Branden Roarke; Greg Alspaugh; Katie A Link; Alessio Andreoni; Mateus P Mori; Paul M Hwang; Dan L Sackett; Jay R Knutson
Journal:  J Biophotonics       Date:  2021-11-16       Impact factor: 3.390

2.  Fluorescence lifetime imaging of metMyoglobin formation due to nitric oxide stress.

Authors:  Rozhin Penjweini; Mateus P Mori; Paul M Hwang; Dan L Sackett; Jay R Knutson
Journal:  Proc SPIE Int Soc Opt Eng       Date:  2022-03-03
  2 in total

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