X-ray absorption studies of intermediates in peroxidase activity

Chance, Britton; Powers, Linda S.; Ching, Yuan-Chin; Poulos, T.L.; Schonbaum, Gregory R.; Yamazaki, Isao; Paul, K. G.

doi:10.1016/0003-9861(84)90234-0

Cited by 164 publications

(173 citation statements)

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“…Bond lengths from the EXAFS studies of CYP119 and its derivatives are listed in Table 2, which also contains previously reported EXAFS results for porphyrin-iron-oxo species (17,(36)(37)(38)(39)(40)(41) and heme-thiolate nitrosyl complexes (42). We note that the errors in EXAFS bond lengths typically are 0.01-0.02 Å.…”

Section: Resultsmentioning

confidence: 89%

“…The relatively long (1.81 Å) iron-oxygen bond in CYP119-II indicates that this compound II derivative likely contains an ironhydroxide moiety. It is in the range of bond lengths predicted computationally for a porphyrin-iron(IV) hydroxide species (48,49), and long iron-oxygen bonds have long been thought to be the signature of protonated ferryl-oxo species in compound II species (36,39,47). Accordingly, one concludes that the ferryloxo species in CYP119-II is basic such that the oxygen atom is protonated at neutral pH.…”

Section: Resultsmentioning

confidence: 96%

“…For compound I species, short iron-oxo bonds (1.64-1.67 Å) were found for the compound I derivative of CPO (37), the compound I derivative of horseradish peroxidase (17,36,39), and the compound I model compounds, 5,10,15,20-tetramesitylporphyrin-iron(IV)-oxo radical cations (36,38). Thus, a short, Ϸ1.65-Å iron-oxygen bond length is the accepted value for ferryl-oxo moieties in compound I species.…”

Section: Resultsmentioning

confidence: 99%

“…Conflicting EXAFS results exist for the iron-oxygen bond length in the compound II derivative of horseradish peroxidase, as shown in Table 2 (17,36,39). EXAFS studies of other compound II analogues indicated short iron-oxygen bonds in a model complex (36), in myoglobin peroxide (40), and in cytochrome c peroxidase ES complex (41), each of which has a ferryl-oxo moiety without a porphyrin radical cation.…”

Section: Resultsmentioning

confidence: 99%

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X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Newcomb

Halgrimson

Horner

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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The cytochrome P450 enzyme CYP119, its compound II derivative, and its nitrosyl complex were studied by iron K-edge x-ray absorption spectroscopy. The compound II derivative was prepared by reaction of the resting enzyme with peroxynitrite and had a lifetime of Ϸ10 s at 23°C. The CYP119 nitrosyl complex was prepared by reaction of the enzyme with nitrogen monoxide gas or with a nitrosyl donor and was stable at 23°C for hours. Samples of CYP119 and its derivatives were studied by x-ray absorption spectroscopy at temperatures below 140 (K) at the Advanced Photon Source of Argonne National Laboratory. The x-ray absorption near-edge structure spectra displayed shifts in edge and pre-edge energies consistent with increasing effective positive charge on iron in the series native CYP119 < CYP119 nitrosyl complex < CYP119 compound II derivative. Extended x-ray absorption fine structure spectra were simulated with good fits for k ‫؍‬ 12 Å ؊1 for native CYP119 and k ‫؍‬ 13 Å ؊1 for both the nitrosyl complex and the compound II derivative. The important structural features for the compound II derivative were an iron-oxygen bond length of 1.82 Å and an iron-sulfur bond length of 2.24 Å, both of which indicate an iron-oxygen single bond in a ferryl-hydroxide, Fe IV OH, moiety.EXAFS ͉ ferryl-oxo ͉ XANES

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Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Newcomb

Halgrimson

Horner

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…Several studies in past years have revealed consistent differences between the structure of the heme in globins and peroxidases [31]. As shown from XAS and high resolution X-ray structures, globins typically have an Fe−N h distance of about 2.1 Å while in the peroxidases this distance is typically shorter by about 0.2 Å, resulting in a typical Fe−N h distance of about 1.9 Å [31][32][33][34][35][36][37][38] (see also Table 3). This was proposed to be crucial to explain the different reactivity observed between the two groups of proteins [34,35].…”

mentioning

confidence: 94%

Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation

Arcovito¹,

Bonamore²,

Hazemann³

et al. 2010

Biophysical Chemistry

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The spectroscopic properties of the deoxygenated truncated hemoglobin from the actinobacterium Thermobifida fusca have been investigated by means of extended X-ray absorption fine structure (EXAFS), X-ray absorption near edge structure (XANES), and near infrared spectroscopies both at room and cryogenic temperatures. At room temperature the near infrared charge transfer band III occurs at 772 nm, a value that is unusually high for a canonical deoxygenated hemoglobin species, and can only be found as a transient species after photolysis in vertebrate hemoglobins and myoglobins or under strongly dehydrating conditions. EXAFS and XANES quantitative analyses, carried out in parallel with deoxygenated horse myoglobin, revealed an unusually short iron-histidine distance 1.90 +/- 0.03 angstrom, significantly shorter than the deoxygenated horse myoglobin distance of 2.11 +/- 0.02 angstrom. These findings provide novel structural basis for discussing the fine structural geometry of the proximal site, and eventually mapping the coordinates of the metal with respect to the pyrrole nitrogens and the proximal histidine nitrogen. (C) 2009 Elsevier B.V. All rights reserved

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Iron: Heme Proteins, Peroxidases, Catalases & Catalase‐PeroxidasesBased in part on the article Iron: Heme Proteins, Peroxidases, & Catalases by Ann M. English which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.

Bhaskar¹,

Lad²,

Poulos³

2005

Encyclopedia of Inorganic Chemistry

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This article describes recent advances made in understanding structure–function relationships in representative peroxidases, catalases, and catalase‐peroxidases. Emphasis will be placed on those enzymes for which crystal structures are available. Of particular interest are recent advances in elucidating the structure of peroxidase compounds I and II, important intermediates that are formed from the reaction of the enzyme with peroxides. The repertoire of known structures in the catalase/peroxidase superfamily now include KatG catalases‐peroxidases and di‐heme peroxidases. These new structures coupled with a wealth of biochemical and biophysical data have provided important new insights into structure and function.

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X-ray absorption studies of intermediates in peroxidase activity

Cited by 164 publications

References 60 publications

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation

Iron: Heme Proteins, Peroxidases, Catalases & Catalase‐PeroxidasesBased in part on the article Iron: Heme Proteins, Peroxidases, & Catalases by Ann M. English which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.

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