Chloroperoxidase. IX. Structure of compound I

Hager, Lowell P.; Doubek, Dennis L.; Silverstein, Robert M.; Hargis, J. H.; Martin, J. C.

doi:10.1021/ja00767a068

Cited by 125 publications

(64 citation statements)

References 6 publications

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“…18 O 2 (m/e ϭ 36) and 16 O 2 (m/e ϭ 32) with no indication of 16 O 18 O (m/e ϭ 34) formation within an experimental error of ϳ3%. This demonstrates that the catalase reactions by the Mb mutants proceed as the deprotonation process of catalase and chloroperoxidase (28,29).…”

Section: O 18 O (M/e ‫؍‬ 34) This Implies That O 2 Is Formed By Two-mentioning

confidence: 82%

Catalase Reaction by Myoglobin Mutants and Native Catalase

Kato

Ueno

Fukuzumi

et al. 2004

Journal of Biological Chemistry

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The catalase reaction has been studied in detail by using myoglobin (Mb) mutants. m/e ‫؍‬ 34). This implies that O 2 is formed by two-electron oxidation of H 2 O 2 without breaking the O™O bond. Deuterium isotope effects on the catalatic reactions of Mb mutants and catalase suggest that the catalatic reactions ofMicrococcus lysodeikticus catalase and F43H/H64L Mb proceed via an ionic mechanism with a small isotope effect of less than 4.0, since the distal histidine residue is located at a proper position to act as a general acid-base catalyst for the ionic reaction. In contrast, other Mb mutants such as H64X (X is Ala, Ser, and Asp) and L29H/H64L Mb oxidize H 2 O 2 via a radical mechanism in which a hydrogen atom is abstracted by Mb-I with a large isotope effect in a range of 10 -29, due to a lack of the general acid-base catalyst.

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Section: O 18 O (M/e ‫؍‬ 34) This Implies That O 2 Is Formed By Two-mentioning

confidence: 82%

Catalase Reaction by Myoglobin Mutants and Native Catalase

Kato

Ueno

Fukuzumi

et al. 2004

Journal of Biological Chemistry

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“…In chloroperoxidase the catalase reaction has been shown to proceed also via a non-scrambling mechanism, whereas in a reaction with labeled and unlabeled m-chloroperoxybenzoic acid a scrambling mechanism for the release of O 2 was established [12]. With m-chloroperoxybenzoic acid the oxygen atoms of O 2 derived from different molecules suggesting that at least one oxygen atom came from compound I (Por Å+ Fe IV ‚O) [12].…”

Section: Introductionmentioning

confidence: 99%

“…With m-chloroperoxybenzoic acid the oxygen atoms of O 2 derived from different molecules suggesting that at least one oxygen atom came from compound I (Por Å+ Fe IV ‚O) [12].…”

Section: Introductionmentioning

confidence: 99%

Hydrogen peroxide oxidation by catalase‐peroxidase follows a non‐scrambling mechanism

et al. 2007

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“…The oxygenated intermediate in hepatic P-450 systems was also resolved with intermediates described in both stopped-flow and steady-state experiments (19)(20)(21)(22). Difficulty in trapping [Fe2+O2] (25,27). Considering ferric heme as +1 and water -2, this state has a total formal charge of 3+.…”

mentioning

confidence: 99%

“…Considering ferric heme as +1 and water -2, this state has a total formal charge of 3+. Much evidence has been accumulated in recent years concerning the actual distribution of charge in compound I of peroxidases, and a feryl iron with a porphyrin cation radical is favored by some workers (27)(28)(29)(30). For [FeO] to the carbon-hydrogen bond of the substrate, a process mechanistically analogous to known carbend and nitrene insertion reactions (31).…”

mentioning

confidence: 99%