1951
DOI: 10.1016/s0021-9258(19)77792-8
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Electrophoretic and Chemical Studies of Canine Pancreatic Juice

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Cited by 10 publications
(1 citation statement)
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“…In proteins, O 2 •– can react with iron–sulfur clusters and heme centers leading to release and/or oxidation of iron . Numerous iron–sulfur cluster- and heme-containing proteins are sensitive to O 2 •– , including aconitase, the bacterial transcription factor SoxR, guanylate cyclase, and myeloperoxidase . Reactivity at protein metal centers is not unique to O 2 •– , however, as metal-dependent peroxide sensors like Bacillus subtilis PerR have also been reported. ,, In contrast to redox switches based on peroxide-sensitive cysteine residues, PerR senses H 2 O 2 by metal-catalyzed oxidation of histidine residues involved in coordinating Fe 2+ (note that the mechanism involves reduction of H 2 O 2 by Fe 2+ to generate • OH, which then reacts rapidly with histidine).…”
Section: Reactive Oxygen Species (Ros) In Biological Systemsmentioning
confidence: 99%
“…In proteins, O 2 •– can react with iron–sulfur clusters and heme centers leading to release and/or oxidation of iron . Numerous iron–sulfur cluster- and heme-containing proteins are sensitive to O 2 •– , including aconitase, the bacterial transcription factor SoxR, guanylate cyclase, and myeloperoxidase . Reactivity at protein metal centers is not unique to O 2 •– , however, as metal-dependent peroxide sensors like Bacillus subtilis PerR have also been reported. ,, In contrast to redox switches based on peroxide-sensitive cysteine residues, PerR senses H 2 O 2 by metal-catalyzed oxidation of histidine residues involved in coordinating Fe 2+ (note that the mechanism involves reduction of H 2 O 2 by Fe 2+ to generate • OH, which then reacts rapidly with histidine).…”
Section: Reactive Oxygen Species (Ros) In Biological Systemsmentioning
confidence: 99%