A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy

James W. A. Allen; Myles R. Cheesman; Christopher W. Higham; Stuart J. Ferguson; Nicholas J. Watmough

doi:10.1006/bbrc.2000.4009

A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy

James W. A. Allen, Myles R. Cheesman, Christopher W. Higham, Stuart J. Ferguson, Nicholas J. Watmough

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

14 Citations (Scopus)

Abstract

Paracoccus pantotrophus cytochrome cd(1) is a physiological nitrite reductase and an in vitro hydroxylamine reductase. The oxidised "as isolated" form of the enzyme has bis-histidinyl coordinated c-heme and upon reduction its coordination changes to histidine/ methionine. Following treatment of reduced enzyme with hydroxylamine, a novel, oxidised, conformer of the enzyme is obtained. We have devised protocols for freeze-quench near-ir-MCD spectroscopy that have allowed us to establish unequivocally the c-heme coordination of this species as His/Met. Thus it is shown that the catalytically competent, hydroxylamine reoxidised, form of P. pantotrophus cytochrome cd(1) has different axial ligands to the c-heme than "as isolated" enzyme. (C) 2000 Academic Press.

Original language	English
Pages (from-to)	674-677
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	279
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.2000.4009
Publication status	Published - 2000

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10.1006/bbrc.2000.4009

Cite this

@article{038c8a67ece54ce184cda598cd289353,

title = "A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy",

abstract = "Paracoccus pantotrophus cytochrome cd(1) is a physiological nitrite reductase and an in vitro hydroxylamine reductase. The oxidised {"}as isolated{"} form of the enzyme has bis-histidinyl coordinated c-heme and upon reduction its coordination changes to histidine/ methionine. Following treatment of reduced enzyme with hydroxylamine, a novel, oxidised, conformer of the enzyme is obtained. We have devised protocols for freeze-quench near-ir-MCD spectroscopy that have allowed us to establish unequivocally the c-heme coordination of this species as His/Met. Thus it is shown that the catalytically competent, hydroxylamine reoxidised, form of P. pantotrophus cytochrome cd(1) has different axial ligands to the c-heme than {"}as isolated{"} enzyme. (C) 2000 Academic Press.",

author = "Allen, {James W. A.} and Cheesman, {Myles R.} and Higham, {Christopher W.} and Ferguson, {Stuart J.} and Watmough, {Nicholas J.}",

year = "2000",

doi = "10.1006/bbrc.2000.4009",

language = "English",

volume = "279",

pages = "674--677",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy. / Allen, James W. A.; Cheesman, Myles R.; Higham, Christopher W.; Ferguson, Stuart J.; Watmough, Nicholas J.

In: Biochemical and Biophysical Research Communications, Vol. 279, No. 2, 2000, p. 674-677.

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

TY - JOUR

T1 - A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy

AU - Allen, James W. A.

AU - Cheesman, Myles R.

AU - Higham, Christopher W.

AU - Ferguson, Stuart J.

AU - Watmough, Nicholas J.

PY - 2000

Y1 - 2000

N2 - Paracoccus pantotrophus cytochrome cd(1) is a physiological nitrite reductase and an in vitro hydroxylamine reductase. The oxidised "as isolated" form of the enzyme has bis-histidinyl coordinated c-heme and upon reduction its coordination changes to histidine/ methionine. Following treatment of reduced enzyme with hydroxylamine, a novel, oxidised, conformer of the enzyme is obtained. We have devised protocols for freeze-quench near-ir-MCD spectroscopy that have allowed us to establish unequivocally the c-heme coordination of this species as His/Met. Thus it is shown that the catalytically competent, hydroxylamine reoxidised, form of P. pantotrophus cytochrome cd(1) has different axial ligands to the c-heme than "as isolated" enzyme. (C) 2000 Academic Press.

AB - Paracoccus pantotrophus cytochrome cd(1) is a physiological nitrite reductase and an in vitro hydroxylamine reductase. The oxidised "as isolated" form of the enzyme has bis-histidinyl coordinated c-heme and upon reduction its coordination changes to histidine/ methionine. Following treatment of reduced enzyme with hydroxylamine, a novel, oxidised, conformer of the enzyme is obtained. We have devised protocols for freeze-quench near-ir-MCD spectroscopy that have allowed us to establish unequivocally the c-heme coordination of this species as His/Met. Thus it is shown that the catalytically competent, hydroxylamine reoxidised, form of P. pantotrophus cytochrome cd(1) has different axial ligands to the c-heme than "as isolated" enzyme. (C) 2000 Academic Press.

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DO - 10.1006/bbrc.2000.4009

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JF - Biochemical and Biophysical Research Communications

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