X-ray absorption studies of intermediates in peroxidase activity

B. Chance; L. Powers; Y. Ching; T. Poulos; G. R. Schonbaum; I. Yamazaki; K. G. Paul

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

X-ray absorption studies of intermediates in peroxidase activity

B. Chance, L. Powers, Y. Ching, T. Poulos, G. R. Schonbaum, I. Yamazaki, K. G. Paul

Electrical and Computer Engineering

Research output: Contribution to journal › Article › peer-review

151 Scopus citations

Abstract

The structures of the enzyme-substrate compounds of peroxidases and catalase determined by X-ray absorption spectroscopy are presented. The valence state of the iron in Compounds I and II is determined from the edge to be higher than Fe⁺³. A short Fe-N_e (proximal histidine) distance is observed in all forms except Compound II, forcing the Fe-N_p average distance to be long, a result which differentiates the peroxidases from the oxygen transport hemoproteins and plays a pivotal role in the mechanism. A correlation is shown between the ratio of peaks in the low k (ligand field indicator ratio) region, the Fe-N_p (heme pyrrole nitrogen) average distance, and the magnetic susceptibility, which provides a sensitive indicator of spin state. The mechanism of H₂O₂ reduction is shown by analysis of the structural changes observed in the intermediates. Possible relationship of these compounds to that of the peroxidatic form of cytochrome oxidase is suggested by these results.

Original language	English (US)
Pages (from-to)	596-611
Number of pages	16
Journal	Archives of Biochemistry and Biophysics
Volume	235
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(84)90234-0
State	Published - Dec 1984

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

Access to Document

10.1016/0003-9861(84)90234-0

Cite this

@article{0da95d812b95409ebac5a088c0bf9798,

title = "X-ray absorption studies of intermediates in peroxidase activity",

abstract = "The structures of the enzyme-substrate compounds of peroxidases and catalase determined by X-ray absorption spectroscopy are presented. The valence state of the iron in Compounds I and II is determined from the edge to be higher than Fe+3. A short Fe-Ne (proximal histidine) distance is observed in all forms except Compound II, forcing the Fe-Np average distance to be long, a result which differentiates the peroxidases from the oxygen transport hemoproteins and plays a pivotal role in the mechanism. A correlation is shown between the ratio of peaks in the low k (ligand field indicator ratio) region, the Fe-Np (heme pyrrole nitrogen) average distance, and the magnetic susceptibility, which provides a sensitive indicator of spin state. The mechanism of H2O2 reduction is shown by analysis of the structural changes observed in the intermediates. Possible relationship of these compounds to that of the peroxidatic form of cytochrome oxidase is suggested by these results.",

author = "B. Chance and L. Powers and Y. Ching and T. Poulos and Schonbaum, {G. R.} and I. Yamazaki and Paul, {K. G.}",

note = "Funding Information: the Division of Materials Research and the National Institutes of Health through the Biotechnology Resource Program in the Division of Research Resources in cooperation with the Department of Energy, Dr. K.-G. Paul{\textquoteright}s was supported by the Swedish Medical Research Council Grant 3X-6522. Funding Information: This work was partially supported Institutes of Health Grants GM-33165, RR-01633, and HL-18{\textquoteright}708; National Science tion Grants PCM-80-26684 and PCM-SO-239{\textquoteright}7% SSRL Projects 660/825B, 659/820B, and ported by the National Science Foundation",

year = "1984",

month = dec,

doi = "10.1016/0003-9861(84)90234-0",

language = "English (US)",

volume = "235",

pages = "596--611",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - X-ray absorption studies of intermediates in peroxidase activity

AU - Chance, B.

AU - Powers, L.

AU - Ching, Y.

AU - Poulos, T.

AU - Schonbaum, G. R.

AU - Yamazaki, I.

AU - Paul, K. G.

N1 - Funding Information: the Division of Materials Research and the National Institutes of Health through the Biotechnology Resource Program in the Division of Research Resources in cooperation with the Department of Energy, Dr. K.-G. Paul’s was supported by the Swedish Medical Research Council Grant 3X-6522. Funding Information: This work was partially supported Institutes of Health Grants GM-33165, RR-01633, and HL-18’708; National Science tion Grants PCM-80-26684 and PCM-SO-239’7% SSRL Projects 660/825B, 659/820B, and ported by the National Science Foundation

PY - 1984/12

Y1 - 1984/12

N2 - The structures of the enzyme-substrate compounds of peroxidases and catalase determined by X-ray absorption spectroscopy are presented. The valence state of the iron in Compounds I and II is determined from the edge to be higher than Fe+3. A short Fe-Ne (proximal histidine) distance is observed in all forms except Compound II, forcing the Fe-Np average distance to be long, a result which differentiates the peroxidases from the oxygen transport hemoproteins and plays a pivotal role in the mechanism. A correlation is shown between the ratio of peaks in the low k (ligand field indicator ratio) region, the Fe-Np (heme pyrrole nitrogen) average distance, and the magnetic susceptibility, which provides a sensitive indicator of spin state. The mechanism of H2O2 reduction is shown by analysis of the structural changes observed in the intermediates. Possible relationship of these compounds to that of the peroxidatic form of cytochrome oxidase is suggested by these results.

AB - The structures of the enzyme-substrate compounds of peroxidases and catalase determined by X-ray absorption spectroscopy are presented. The valence state of the iron in Compounds I and II is determined from the edge to be higher than Fe+3. A short Fe-Ne (proximal histidine) distance is observed in all forms except Compound II, forcing the Fe-Np average distance to be long, a result which differentiates the peroxidases from the oxygen transport hemoproteins and plays a pivotal role in the mechanism. A correlation is shown between the ratio of peaks in the low k (ligand field indicator ratio) region, the Fe-Np (heme pyrrole nitrogen) average distance, and the magnetic susceptibility, which provides a sensitive indicator of spin state. The mechanism of H2O2 reduction is shown by analysis of the structural changes observed in the intermediates. Possible relationship of these compounds to that of the peroxidatic form of cytochrome oxidase is suggested by these results.

UR - http://www.scopus.com/inward/record.url?scp=0021670303&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021670303&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(84)90234-0

DO - 10.1016/0003-9861(84)90234-0

M3 - Article

C2 - 6097192

AN - SCOPUS:0021670303

SN - 0003-9861

VL - 235

SP - 596

EP - 611

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 2

ER -

X-ray absorption studies of intermediates in peroxidase activity

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this