1975
DOI: 10.1016/0005-2795(75)90091-4
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Induced changes in the electron paramagnetic resonance spectra of mammalian catalases

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Cited by 25 publications
(11 citation statements)
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“…Furthermore, other features on either side of the feature at g = 6.0 could also be detected, at g 6.33, 5.45. We provisionally assign these features to active catalase A high-spin haem, for the following reasons: (a) the gvalues are very similar to those of isolated rat liver, bovine liver and human erythrocyte catalase, and (b) the spectrum could be modified by the addition of formate (see Figure 6b), which is a peroxidative substrate for catalase, binding to the enzyme as the free acid to give catalase B (g 6.8, 5.0) [39].…”
Section: Resultsmentioning
confidence: 88%
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“…Furthermore, other features on either side of the feature at g = 6.0 could also be detected, at g 6.33, 5.45. We provisionally assign these features to active catalase A high-spin haem, for the following reasons: (a) the gvalues are very similar to those of isolated rat liver, bovine liver and human erythrocyte catalase, and (b) the spectrum could be modified by the addition of formate (see Figure 6b), which is a peroxidative substrate for catalase, binding to the enzyme as the free acid to give catalase B (g 6.8, 5.0) [39].…”
Section: Resultsmentioning
confidence: 88%
“…Treatment with either succinate, ascorbate/ TMPD or dithionite resulted in similar spectra containing contributions from both catalases A and B, although the intensities of the two species are clearly different, with catalase A still dominating the low-field region of succinate-reduced membranes ( Figure 6a). The shift in the g-values provisionally assigned to catalase A, to g = 6.8 and 5.0, on treatment of mitochondrial membranes with formate, is typically observed upon formation of the catalase-formate complex, catalase B, and is probably due to a change in the rhombicity of iron (Figure 6b) [39]. Reduction of the formate-treated sample resulted in the total disappearance of the g = 6.0 haem EPR signal, thereby enhancing the-features due to catalase B, which is only slowly reduced by dithionite (Figure 6b).…”
Section: Littoralls Fat-body Miochondrial Membranesmentioning
confidence: 95%
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“…This observation confirms that the substrate does not modify the heme coordination and electronic structures in the ferric form. The signal at g = 4.30 observed for C357H is likely to be derived from free iron, which could not be removed by the present purification for C357H [56]. The EPR signals of the ferric mutant was insensitive to pH changes between 6 and 10 (results not shown), implying that the sixth ligand is not a hydroxide anion.…”
Section: Resultsmentioning
confidence: 91%
“…The Fe 3+ /Fe 2+ couples are −230 mV in H93C Mb and −190 mV in H93Y Mb, whereas the couple for wild type Mb is +50 mV. The redox potential change in the mutants can be interpreted in terms of stabilizing the ferric heme iron with the negatively charged thiolate from cysteine or phenolate from tyrosine [21][22][23][24]. When wild type Mb is treated with cumene hydroperoxide oxidant, the oxidation proceeds by both heterolytic and hemolytic reaction mechanisms to form (porph + • )Fe IV [20].…”
Section: The Structures and Reactivities Of Compound I (Porph + • )Fementioning
confidence: 99%