Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119

Ilia G. Denisov; Shao Ching Hung; Kara E. Weiss; Mark A. McLean; Yoshitsugu Shiro; Sam Yong Park; Paul M. Champion; Stephen G. Sligar

doi:10.1016/S0162-0134(01)00328-2

Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119

Ilia G. Denisov, Shao Ching Hung, Kara E. Weiss, Mark A. McLean, Yoshitsugu Shiro, Sam Yong Park, Paul M. Champion, Stephen G. Sligar

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

Abstract

Using UV-Vis, resonance Raman, and EPR spectroscopy we have studied the properties of the oxygenated ferrous cytochrome P450 from Sulfolobus Solfataricus, (CYP119). The recently determined crystal structure of CYP119 is compared with other available structures of P450s, and detailed structural and spectroscopic analyses are reported. With several structural similarities to CYP102, such as in-plane iron position and a shorter iron-proximal ligand bond, CYP119 shows low-spin conformation preference in the ferric form and partially in the ferrous form at low temperatures. These structural features can explain the fast autoxidation of the oxyferrous complex of CYP119. Finally, we report the first UV-Vis and EPR spectra of the cryoradiolytically reduced oxygenated intermediate of CYP119. The primary reduced intermediate, a hydroperoxo-ferric complex of CYP119, undergoes a 'peroxide shunt' pathway during gradual annealing at 170-195 K and returns to the low-spin ferric form.

Original language	English (US)
Pages (from-to)	215-226
Number of pages	12
Journal	Journal of Inorganic Biochemistry
Volume	87
Issue number	4
DOIs	https://doi.org/10.1016/S0162-0134(01)00328-2
State	Published - Dec 15 2001

Keywords

Cryoradiolytic reduction
Cytochrome P450
Low temperature spectroscopy
Oxyferrous heme complex

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

Online availability

10.1016/S0162-0134(01)00328-2

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@article{a2812a1c39ff4bd9a90de1f97bc27ddf,

title = "Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119",

abstract = "Using UV-Vis, resonance Raman, and EPR spectroscopy we have studied the properties of the oxygenated ferrous cytochrome P450 from Sulfolobus Solfataricus, (CYP119). The recently determined crystal structure of CYP119 is compared with other available structures of P450s, and detailed structural and spectroscopic analyses are reported. With several structural similarities to CYP102, such as in-plane iron position and a shorter iron-proximal ligand bond, CYP119 shows low-spin conformation preference in the ferric form and partially in the ferrous form at low temperatures. These structural features can explain the fast autoxidation of the oxyferrous complex of CYP119. Finally, we report the first UV-Vis and EPR spectra of the cryoradiolytically reduced oxygenated intermediate of CYP119. The primary reduced intermediate, a hydroperoxo-ferric complex of CYP119, undergoes a 'peroxide shunt' pathway during gradual annealing at 170-195 K and returns to the low-spin ferric form.",

keywords = "Cryoradiolytic reduction, Cytochrome P450, Low temperature spectroscopy, Oxyferrous heme complex",

author = "Denisov, {Ilia G.} and Hung, {Shao Ching} and Weiss, {Kara E.} and McLean, {Mark A.} and Yoshitsugu Shiro and Park, {Sam Yong} and Champion, {Paul M.} and Sligar, {Stephen G.}",

note = "Funding Information: We gratefully appreciate the constant support and help provided by Dr. John Bentley while using the cobalt-60 source in the Notre Dame Radiation Laboratory (Notre Dame University, IN, USA). Irradiations were conducted at the Notre Dame Radiation Laboratory, which is a facility of the US Department of Energy, Office of Basic Energy Sciences. Many fruitful and friendly discussions with Dr. S.A. Maves during the early stage of this work were useful and helpful. NIH Research Resources Grant P-41-RR01811 is acknowledged for the use of IERC resources. The work was supported by grants from the National Institute of Health GM33775 and GM31756 to S.G. Sligar, and by grants from NIH DK-35090 and from NSF MCB-9904516 to P.M. Champion.",

year = "2001",

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doi = "10.1016/S0162-0134(01)00328-2",

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TY - JOUR

T1 - Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119

AU - Denisov, Ilia G.

AU - Hung, Shao Ching

AU - Weiss, Kara E.

AU - McLean, Mark A.

AU - Shiro, Yoshitsugu

AU - Park, Sam Yong

AU - Champion, Paul M.

AU - Sligar, Stephen G.

N1 - Funding Information: We gratefully appreciate the constant support and help provided by Dr. John Bentley while using the cobalt-60 source in the Notre Dame Radiation Laboratory (Notre Dame University, IN, USA). Irradiations were conducted at the Notre Dame Radiation Laboratory, which is a facility of the US Department of Energy, Office of Basic Energy Sciences. Many fruitful and friendly discussions with Dr. S.A. Maves during the early stage of this work were useful and helpful. NIH Research Resources Grant P-41-RR01811 is acknowledged for the use of IERC resources. The work was supported by grants from the National Institute of Health GM33775 and GM31756 to S.G. Sligar, and by grants from NIH DK-35090 and from NSF MCB-9904516 to P.M. Champion.

PY - 2001/12/15

Y1 - 2001/12/15

N2 - Using UV-Vis, resonance Raman, and EPR spectroscopy we have studied the properties of the oxygenated ferrous cytochrome P450 from Sulfolobus Solfataricus, (CYP119). The recently determined crystal structure of CYP119 is compared with other available structures of P450s, and detailed structural and spectroscopic analyses are reported. With several structural similarities to CYP102, such as in-plane iron position and a shorter iron-proximal ligand bond, CYP119 shows low-spin conformation preference in the ferric form and partially in the ferrous form at low temperatures. These structural features can explain the fast autoxidation of the oxyferrous complex of CYP119. Finally, we report the first UV-Vis and EPR spectra of the cryoradiolytically reduced oxygenated intermediate of CYP119. The primary reduced intermediate, a hydroperoxo-ferric complex of CYP119, undergoes a 'peroxide shunt' pathway during gradual annealing at 170-195 K and returns to the low-spin ferric form.

AB - Using UV-Vis, resonance Raman, and EPR spectroscopy we have studied the properties of the oxygenated ferrous cytochrome P450 from Sulfolobus Solfataricus, (CYP119). The recently determined crystal structure of CYP119 is compared with other available structures of P450s, and detailed structural and spectroscopic analyses are reported. With several structural similarities to CYP102, such as in-plane iron position and a shorter iron-proximal ligand bond, CYP119 shows low-spin conformation preference in the ferric form and partially in the ferrous form at low temperatures. These structural features can explain the fast autoxidation of the oxyferrous complex of CYP119. Finally, we report the first UV-Vis and EPR spectra of the cryoradiolytically reduced oxygenated intermediate of CYP119. The primary reduced intermediate, a hydroperoxo-ferric complex of CYP119, undergoes a 'peroxide shunt' pathway during gradual annealing at 170-195 K and returns to the low-spin ferric form.

KW - Cryoradiolytic reduction

KW - Cytochrome P450

KW - Low temperature spectroscopy

KW - Oxyferrous heme complex

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U2 - 10.1016/S0162-0134(01)00328-2

DO - 10.1016/S0162-0134(01)00328-2

M3 - Article

C2 - 11744059

AN - SCOPUS:0035893829

SN - 0162-0134

VL - 87

SP - 215

EP - 226

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

IS - 4

ER -

Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119

Abstract

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