The Mechanism of Metmyoglobin Oxidation

King, N. Kelso; Winfield, ME

doi:10.1016/s0021-9258(18)81216-9

Cited by 267 publications

(67 citation statements)

References 18 publications

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“…1). These new absorption bands are attributed to the ferryloxo (Fe(IV)=O) species [8,9]. When the Fe(IV)=O species is produced in methMb by H2O2, the porphyrin π-cation radical is generated concomitantly [8][9][10]12] and amino acid radicals are formed by intramolecular electron transfer from the amino acid residue to the porphyrin π-cation radical [11].…”

Section: Formation Of the Fe(iv)=o Species In Hmb By Reaction With H2o2mentioning

confidence: 99%

“…These new absorption bands are attributed to the ferryloxo (Fe(IV)=O) species [8,9]. When the Fe(IV)=O species is produced in methMb by H2O2, the porphyrin π-cation radical is generated concomitantly [8][9][10]12] and amino acid radicals are formed by intramolecular electron transfer from the amino acid residue to the porphyrin π-cation radical [11]. The pseudo-first-order rate constants (kobs(Fe(IV))) of Fe(IV)=O formation for WT and C110A methMbs under air were obtained by fitting the absorbance changes at 421 nm with single-exponential functions.…”

Section: Formation Of the Fe(iv)=o Species In Hmb By Reaction With H2o2mentioning

confidence: 99%

“…The reaction of Mb with H2O2 has also been investigated extensively [6][7][8][9][10][11][12][13]. The ferryloxo (Fe(IV)=O) species is generated by the reaction of metMb with H2O2, where an electron is provided to the heme iron from the porphyrin or nearby amino acid and thus a porphyrin π-cation radical or amino acid radical is produced, respectively.…”

Section: Introductionmentioning

confidence: 99%

“…The ferryloxo (Fe(IV)=O) species is generated by the reaction of metMb with H2O2, where an electron is provided to the heme iron from the porphyrin or nearby amino acid and thus a porphyrin π-cation radical or amino acid radical is produced, respectively. The ferryloxo species with and without the π-cation is referred to as compound I and compound II, respectively [7][8][9][10]. Locations of the amino acid radicals in compound II of sperm whale and human Mbs have been investigated with EPR using the spin-trapping technique [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Nagao

Asami

Yasui

et al. 2011

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Section: Formation Of the Fe(iv)=o Species In Hmb By Reaction With H2o2mentioning

confidence: 99%

Section: Formation Of the Fe(iv)=o Species In Hmb By Reaction With H2o2mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Nagao

Asami

Yasui

et al. 2011

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…A decrease in the Soret band does not always indicate heme degradation, because reaction intermediates of hemoproteins with H 2 O 2 called as compound I (Fe IV =O +• ), compound ES (Fe IV =O/amino acid radical) and compound II (Fe IV =O) are known to have features of a relatively weak Soret band [40,41]. The reaction of myoglobin with H 2 O 2 resulted in a decrease in the intensity of the Soret band (Fig.…”

Section: Heme-degradation Activity Of the K164h Mutantmentioning

confidence: 99%

A single mutation converts Alr5027 from cyanobacteria Nostoc sp. PCC 7120 to a heme-binding protein with heme-degrading ability

Dojun

Muranishi

Ishimori

et al. 2020

Journal of Inorganic Biochemistry

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Heme Proteins and Model Systems

Ozaki

Watanabe

2002

Encyclopedia of Catalysis

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This article describes mechanistic aspects of the active intermediate formation and a variety of reactions catalyzed by peroxidases. In two‐electron oxidations, a ferryl porphyrin π‐cation radical intermediate (the so‐called compound I) is generally involved, while one‐electron oxidation of substrates such as amines and phenols could proceed even when the active species is compound II, which is one‐electron reduced form of compound I (Fe IV O species). Many efforts have been made to utilize peroxidases as two‐electron oxidants rather than one‐electron oxidation cataysts. Site‐directed mutagenesis of peroxidases and myoglobin to construct highly efficient and enantioselective oxidation catalysts is an example of these efforts. In addition, random mutagenesis coupled with screening is a way of directed evolution to find biocatalysts suitable for desired oxidations. Chemical modification of amino acid residues and the heme prosthetic group is also an important strategy for the construction of enzymatic activities that are very different from those of the native enzymatic reactions.

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The Mechanism of Metmyoglobin Oxidation

Cited by 267 publications

References 18 publications

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

Efficient reduction of Cys110 thiyl radical by glutathione in human myoglobin

A single mutation converts Alr5027 from cyanobacteria Nostoc sp. PCC 7120 to a heme-binding protein with heme-degrading ability

Heme Proteins and Model Systems

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