Mössbauer- and EPR-Snapshots of an enzymatic reaction: The cytochrome P450 reaction cycle

V. Schünemann; C. Jung; F. Lendzian; A. L. Barra; T. Teschner; A. X. Trautwein

doi:10.1023/B:HYPE.0000043237.03194.72

Mössbauer- and EPR-Snapshots of an enzymatic reaction: The cytochrome P450 reaction cycle

V. Schünemann^*, C. Jung, F. Lendzian, A. L. Barra, T. Teschner, A. X. Trautwein

^*Korrespondierende/r Autor/-in für diese Arbeit

11 Zitate (Scopus)

Abstract

In this communication we present a complimentary Mössbauer- and EPR-study of the time dependance of the reaction of substrate free P450cam with peracetic acid within a time region ranging from 8 ms up to 5 min. An Fe(IV) species as well as a tyrosyl radical residing on the amino acid residue Tyr96 have been identified as reaction intermediates. These species possibly are formed by the reduction of compound I by means of transferring an electron from Tyr 96 to the heme moiety.

Originalsprache	Englisch
Zeitschrift	Hyperfine Interactions
Jahrgang	156-157
Ausgabenummer	1-4
Seiten (von - bis)	247-256
Seitenumfang	10
ISSN	0304-3843
DOIs	https://doi.org/10.1023/B:HYPE.0000043237.03194.72
Publikationsstatus	Veröffentlicht - 01.03.2004

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10.1023/B:HYPE.0000043237.03194.72

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title = "M{\"o}ssbauer- and EPR-Snapshots of an enzymatic reaction: The cytochrome P450 reaction cycle",

abstract = "In this communication we present a complimentary M{\"o}ssbauer- and EPR-study of the time dependance of the reaction of substrate free P450cam with peracetic acid within a time region ranging from 8 ms up to 5 min. An Fe(IV) species as well as a tyrosyl radical residing on the amino acid residue Tyr96 have been identified as reaction intermediates. These species possibly are formed by the reduction of compound I by means of transferring an electron from Tyr 96 to the heme moiety.",

author = "V. Sch{\"u}nemann and C. Jung and F. Lendzian and Barra, \{A. L.\} and T. Teschner and Trautwein, \{A. X.\}",

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doi = "10.1023/B:HYPE.0000043237.03194.72",

language = "English",

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T1 - Mössbauer- and EPR-Snapshots of an enzymatic reaction: The cytochrome P450 reaction cycle

AU - Schünemann, V.

AU - Jung, C.

AU - Lendzian, F.

AU - Barra, A. L.

AU - Teschner, T.

AU - Trautwein, A. X.

PY - 2004/3/1

Y1 - 2004/3/1

N2 - In this communication we present a complimentary Mössbauer- and EPR-study of the time dependance of the reaction of substrate free P450cam with peracetic acid within a time region ranging from 8 ms up to 5 min. An Fe(IV) species as well as a tyrosyl radical residing on the amino acid residue Tyr96 have been identified as reaction intermediates. These species possibly are formed by the reduction of compound I by means of transferring an electron from Tyr 96 to the heme moiety.

AB - In this communication we present a complimentary Mössbauer- and EPR-study of the time dependance of the reaction of substrate free P450cam with peracetic acid within a time region ranging from 8 ms up to 5 min. An Fe(IV) species as well as a tyrosyl radical residing on the amino acid residue Tyr96 have been identified as reaction intermediates. These species possibly are formed by the reduction of compound I by means of transferring an electron from Tyr 96 to the heme moiety.

UR - https://www.scopus.com/pages/publications/27544492037

U2 - 10.1023/B:HYPE.0000043237.03194.72

DO - 10.1023/B:HYPE.0000043237.03194.72

M3 - Journal articles

AN - SCOPUS:27544492037

SN - 0304-3843

VL - 156-157

SP - 247

EP - 256

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Mössbauer- and EPR-Snapshots of an enzymatic reaction: The cytochrome P450 reaction cycle

Abstract

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