Spectroscopic Evidence for a Heme-Heme Binuclear Center in the Cytochrome bd Ubiquinol Oxidase from Escherichia coli
The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. This enzyme is structurally unrelated to the heme-Cu oxidases such as cytochrome c oxidase. While the cytochrome bd complex contains no copper, it does have three heme prosthetic gro...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 90; no. 12; pp. 5863 - 5867 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
National Academy of Sciences of the United States of America
15.06.1993
National Acad Sciences National Academy of Sciences |
Subjects | |
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Abstract | The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. This enzyme is structurally unrelated to the heme-Cu oxidases such as cytochrome c oxidase. While the cytochrome bd complex contains no copper, it does have three heme prosthetic groups: heme b558, heme b595, and heme d (a chlorin). Heme b558appears to be involved in the oxidation of quinol, and heme d is known to be the site where oxygen binds and is reduced to water. The role of heme b595, which is high spin, is not known. In this paper, CO is used to probe the oxygen-binding site by use of Fourier transform infrared spectroscopy to monitor the stretching frequency of CO bound to the enzyme. Photodissociation at low temperature (e.g., 20 K) of the CO-heme d adduct results in CO associated with the protein within the heme binding pocket. This photodissociated CO can subsequently relax to form a kinetically trapped CO-heme b595adduct. The data clearly show that heme d and heme b595must reside within a common binding pocket in the enzyme. The catalytic active site where oxygen is reduced to water is, thus, properly considered to be a heme d-heme b595binuclear center. This is analogous to the heme a3-CuBbinuclear center in the heme-Cu oxidases. Heme b595may play roles analogous to those proposed for the CuBcomponent of cytochrome c oxidase. |
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AbstractList | The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. This enzyme is structurally unrelated to the heme-Cu oxidases such as cytochrome c oxidase. While the cytochrome bd complex contains no copper, it does have three heme prosthetic groups: heme b558, heme b595, and heme d (a chlorin). Heme b558 appears to be involved in the oxidation of quinol, and heme d is known to be the site where oxygen binds and is reduced to water. The role of heme b595, which is high spin, is not known. In this paper, CO is used to probe the oxygen-binding site by use of Fourier transform infrared spectroscopy to monitor the stretching frequency of CO bound to the enzyme. Photodissociation at low temperature (e.g., 20 K) of the CO-heme d adduct results in CO associated with the protein within the heme binding pocket. This photodissociated CO can subsequently relax to form a kinetically trapped CO-heme b595 adduct. The data clearly show that heme d and heme b595 must reside within a common binding pocket in the enzyme. The catalytic active site where oxygen is reduced to water is, thus, properly considered to be a heme d-heme b595 binuclear center. This is analogous to the heme alpha 3-Cu(B) binuclear center in the heme-Cu oxidases. Heme b595 may play roles analogous to those proposed for the Cu(B) component of cytochrome c oxidase. The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli . This enzyme is structurally unrelated to the heme-Cu oxidases such as cytochrome c oxidase. While the cytochrome bd complex contains no copper, it does have three heme prosthetic groups: heme b sub(558), heme b sub(595), and heme d (a chlorin). Heme b sub(558) appears to be involved in the oxidation of quinol, and heme d is known to be the site where oxygen binds and is reduced to water. The role of heme b sub(595), which is high spin, is not known. In this paper, CO is used to probe the oxygen-binding site by use of Fourier transform infrared spectroscopy to monitor the stretching frequency of CO bound to the enzyme. Photodissociation at low temperature (e.g., 20 K) of the CO-heme d adduct results in CO associated with the protein within the heme binding pocket. This photodissociated CO can subsequently relax to form a kinetically trapped CO-heme b sub(595) adduct. The data clearly show that heme d and heme b sub(595) must reside within a common binding pocket in the enzyme. The catalytic active site where oxygen is reduced to water is, thus, properly considered to be a heme d-heme b sub(595) binuclear center. This is analogous to the heme a sub(3)-Cu sub(B) binuclear center in the heme-Cu oxidases. Heme b sub(595) may play roles analogous to those proposed for the Cu sub(B) component of cytochrome c oxidase. The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. This enzyme is structurally unrelated to the heme-Cu oxidases such as cytochrome c oxidase. While the cytochrome bd complex contains no copper, it does have three heme prosthetic groups: heme b558, heme b595, and heme d (a chlorin). Heme b558appears to be involved in the oxidation of quinol, and heme d is known to be the site where oxygen binds and is reduced to water. The role of heme b595, which is high spin, is not known. In this paper, CO is used to probe the oxygen-binding site by use of Fourier transform infrared spectroscopy to monitor the stretching frequency of CO bound to the enzyme. Photodissociation at low temperature (e.g., 20 K) of the CO-heme d adduct results in CO associated with the protein within the heme binding pocket. This photodissociated CO can subsequently relax to form a kinetically trapped CO-heme b595adduct. The data clearly show that heme d and heme b595must reside within a common binding pocket in the enzyme. The catalytic active site where oxygen is reduced to water is, thus, properly considered to be a heme d-heme b595binuclear center. This is analogous to the heme a3-CuBbinuclear center in the heme-Cu oxidases. Heme b595may play roles analogous to those proposed for the CuBcomponent of cytochrome c oxidase. The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. The role of heme b595, a heme prosthetic group of the cytochrome bd complex, is not known. Carbon monoxide (CO) is used to probe the oxygen-binding site by use of Fourier transform infrared spectroscopy to monitor the stretching frequency of CO bound to the enzyme. |
Author | Alben, James O. Gennis, Robert B. Hill, John J. |
AuthorAffiliation | School of Chemical Sciences, University of Illinois, Urbana 61801 |
AuthorAffiliation_xml | – name: School of Chemical Sciences, University of Illinois, Urbana 61801 |
Author_xml | – sequence: 1 givenname: John J. surname: Hill fullname: Hill, John J. – sequence: 2 givenname: James O. surname: Alben fullname: Alben, James O. – sequence: 3 givenname: Robert B. surname: Gennis fullname: Gennis, Robert B. |
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Keywords | Cytochrome Fourier transformation Molecular structure Escherichia coli Aerobe Photodissociation Proteins Infrared spectrometry Heme Bacteria Carbon monoxide Enterobacteriaceae Cell respiration |
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Snippet | The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. This enzyme is structurally unrelated to... The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli. The role of heme b595, a heme prosthetic... The cytochrome bd complex is a ubiquinol oxidase, which is part of the aerobic respiratory chain of Escherichia coli . This enzyme is structurally unrelated to... |
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SubjectTerms | Absorption spectra Adducts Analytical, structural and metabolic biochemistry Bacteria Binding Sites Biochemistry Biological and medical sciences Carbon Dioxide - metabolism Cellular biology Cytochromes Cytochromes - chemistry Cytochromes - metabolism Electron Transport Chain Complex Proteins Enzymes Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Heme - metabolism Light Low temperature Models, Structural Oxidases Oxidoreductases Oxidoreductases - chemistry Oxidoreductases - metabolism Oxygen Photolysis Physics Protein Conformation Scientific imaging Spectrophotometry - methods Spectrophotometry, Infrared - methods Visible spectrum |
Title | Spectroscopic Evidence for a Heme-Heme Binuclear Center in the Cytochrome bd Ubiquinol Oxidase from Escherichia coli |
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