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10.1089/ars.2012.4887 http://scihub22266oqcxt.onion/10.1089/ars.2012.4887 C3638515!3638515 !22900975     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\22900975 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Antioxid+Redox+Signal 2013 ; 18 (17 ): 2342-51 Nephropedia Template TP {{tp|p=22900975 |t=2013. Redox reactions of myoglobin |pdf=|usr=}}{{22900975 }} gab.com Text Redox reactions of myoglobin JO: Antioxid Redox Signal http://www.kidney.de/pget.php?&tw=1&pmid=22900975 #FOAvip SIGNIFICANCE: Failure to maintain myoglobin (Mb) in the reduced state causes the formation of metMb, ferryl Mb species, and cross-linked Mb. Dissociation of ferriprotoporphyrin IX from the globin and release of iron atoms can also occur as oxidized Mb accumulates. These modifications may contribute to various oxidative pathologies in muscle and muscle foods. RECENT ADVANCES: The mechanism of ferryl Mb-mediated oxidative damage to nearby structures has been partially elucidated. Dissociation of ferriprotoporphyrin IX from metMb occurs more readily at acidic pH values. The dissociated ferriprotoporphyrin IX (also called hemin) readily decomposes preformed lipid hydroperoxides to reactive oxygen species. Heme oxygenase as well as lipophilic free radicals can degrade the protoporphyrin IX moiety, which results in the formation of free iron. CRITICAL ISSUES: The multiple pathways by which Mb can incur toxicity create difficulties in determining the major cause of oxidative damage in a particular system. Peroxides and low pH activate each of the oxidative Mb forms, ferriprotoporphyrin IX, and released iron. Determining the relative concentration of these species is technically difficult, but essential to a complete understanding of oxidative pathology in muscle tissue. FUTURE DIRECTIONS: Improved methods to assess the different pathways of Mb toxicity are needed. Although significant advances have been made in the understanding of Mb interactions with other biomolecules, further investigation is needed to understand the physical and chemical nature of these interactions. Twit Text FOAVip Redox reactions of myoglobin ????Antioxid Redox Signal http://www.kidney.de/pget.php?&tw=1&pmid=22900975 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=22900975 #FOAvip English Wikipedia <ref>{{Cite pmid|22900975 }}</ref> Redox reactions of myoglobin #MMPMID22900975 Richards MP Antioxid Redox Signal 2013[Jun]; 18 (17 ): 2342-51 PMID22900975 show ga SIGNIFICANCE: Failure to maintain myoglobin (Mb) in the reduced state causes the formation of metMb, ferryl Mb species, and cross-linked Mb. Dissociation of ferriprotoporphyrin IX from the globin and release of iron atoms can also occur as oxidized Mb accumulates. These modifications may contribute to various oxidative pathologies in muscle and muscle foods. RECENT ADVANCES: The mechanism of ferryl Mb-mediated oxidative damage to nearby structures has been partially elucidated. Dissociation of ferriprotoporphyrin IX from metMb occurs more readily at acidic pH values. The dissociated ferriprotoporphyrin IX (also called hemin) readily decomposes preformed lipid hydroperoxides to reactive oxygen species. Heme oxygenase as well as lipophilic free radicals can degrade the protoporphyrin IX moiety, which results in the formation of free iron. CRITICAL ISSUES: The multiple pathways by which Mb can incur toxicity create difficulties in determining the major cause of oxidative damage in a particular system. Peroxides and low pH activate each of the oxidative Mb forms, ferriprotoporphyrin IX, and released iron. Determining the relative concentration of these species is technically difficult, but essential to a complete understanding of oxidative pathology in muscle tissue. FUTURE DIRECTIONS: Improved methods to assess the different pathways of Mb toxicity are needed. Although significant advances have been made in the understanding of Mb interactions with other biomolecules, further investigation is needed to understand the physical and chemical nature of these interactions. |Hemin/metabolism [MESH] |Humans [MESH] |Iron/metabolism [MESH] |Myoglobin/chemistry/*metabolism [MESH] |Oxidation-Reduction [MESH] |Peroxides/metabolism [MESH]Redox reactions of myoglobin (epmc).pdf DeepDyve Pubget Overpricing