Proposed Structure for the Prosthetic Group of the Catalase HPII from Escherichia coli

Peter C. Loewen; Jacek Switala; Jen Ting Chiu; Russell Timkovich; Robert B. Gennis

doi:10.1021/ja00200a023

Proposed Structure for the Prosthetic Group of the Catalase HPII from Escherichia coli

Peter C. Loewen, Jacek Switala, Jen Ting Chiu, Russell Timkovich, Robert B. Gennis

Biochemistry

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

Abstract

Escherichia coli contains two catalases designated HPI and HPII. The heme prosthetic group of HPII is an unusual green chromophore that was believed to be a member of the family of d-type hemes. The heme was extracted and compared to the heme of the terminal oxidase cytochrome complex in E. coli. The two hemes were very similar by visible spectroscopy but were resolved by chromatography. The heme was converted to a free-base, esterified derivative that was characterized by ¹H NMR spectroscopy, infrared spectroscopy, and mass spectrometry. The proposed structure for the free base is 12-hydroxy-13-cis-spirolactone-2, 7, 12, 18-tetramethyl-3, 8-divinyl-17-propionylporphyrin.

Original language	English (US)
Pages (from-to)	7046-7050
Number of pages	5
Journal	Journal of the American Chemical Society
Volume	111
Issue number	18
DOIs	https://doi.org/10.1021/ja00200a023
State	Published - Aug 1 1989

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja00200a023

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abstract = "Escherichia coli contains two catalases designated HPI and HPII. The heme prosthetic group of HPII is an unusual green chromophore that was believed to be a member of the family of d-type hemes. The heme was extracted and compared to the heme of the terminal oxidase cytochrome complex in E. coli. The two hemes were very similar by visible spectroscopy but were resolved by chromatography. The heme was converted to a free-base, esterified derivative that was characterized by 1H NMR spectroscopy, infrared spectroscopy, and mass spectrometry. The proposed structure for the free base is 12-hydroxy-13-cis-spirolactone-2, 7, 12, 18-tetramethyl-3, 8-divinyl-17-propionylporphyrin.",

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AU - Loewen, Peter C.

AU - Switala, Jacek

AU - Chiu, Jen Ting

AU - Timkovich, Russell

AU - Gennis, Robert B.

PY - 1989/8/1

Y1 - 1989/8/1

N2 - Escherichia coli contains two catalases designated HPI and HPII. The heme prosthetic group of HPII is an unusual green chromophore that was believed to be a member of the family of d-type hemes. The heme was extracted and compared to the heme of the terminal oxidase cytochrome complex in E. coli. The two hemes were very similar by visible spectroscopy but were resolved by chromatography. The heme was converted to a free-base, esterified derivative that was characterized by 1H NMR spectroscopy, infrared spectroscopy, and mass spectrometry. The proposed structure for the free base is 12-hydroxy-13-cis-spirolactone-2, 7, 12, 18-tetramethyl-3, 8-divinyl-17-propionylporphyrin.

AB - Escherichia coli contains two catalases designated HPI and HPII. The heme prosthetic group of HPII is an unusual green chromophore that was believed to be a member of the family of d-type hemes. The heme was extracted and compared to the heme of the terminal oxidase cytochrome complex in E. coli. The two hemes were very similar by visible spectroscopy but were resolved by chromatography. The heme was converted to a free-base, esterified derivative that was characterized by 1H NMR spectroscopy, infrared spectroscopy, and mass spectrometry. The proposed structure for the free base is 12-hydroxy-13-cis-spirolactone-2, 7, 12, 18-tetramethyl-3, 8-divinyl-17-propionylporphyrin.

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Proposed Structure for the Prosthetic Group of the Catalase HPII from Escherichia coli

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