Literature DB >> 5917210

Products of methemoglobin oxidation at acid pH.

N K King, M E Winfield.   

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Year:  1966        PMID： 5917210

Source DB:  PubMed          Journal:  Aust J Biol Sci        ISSN： 0004-9417


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  3 in total

1.  Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase.

Authors:  Y Osawa; K Korzekwa
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-15       Impact factor: 11.205

2.  pH-dependent forms of the ferryl haem in myoglobin peroxide analysed by variable-temperature magnetic circular dichroism.

Authors:  N Foote; P M Gadsby; C Greenwood; A J Thomson
Journal:  Biochem J       Date:  1989-07-15       Impact factor: 3.857

3.  Hydrogen peroxide-mediated alteration of the heme prosthetic group of metmyoglobin to an iron chlorin product: evidence for a novel oxidative pathway.

Authors:  K Sugiyama; R J Highet; A Woods; R J Cotter; Y Osawa
Journal:  Proc Natl Acad Sci U S A       Date:  1997-02-04       Impact factor: 11.205
  3 in total

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