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Title: Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria

Abstract

The carbon monoxide oxidases (COXs) purified from the carboxydotrophic bacteria Pseudomonas carboxydohydrogena and Pseudomonas carboxydoflava were found to be molybdenum hydroxylases, identical in cofactor composition and spectral properties to the recently characterized enzyme from Pseudomonas carboxydovorans. All three enzymes exhibited a cofactor composition of two flavin adenine dinucleotides, two molybdenums, eight irons and eight labile sulfides per dimeric molecule, typical for molybdenum-containing iron-sulfur flavoproteins. The millimolar extinction coefficient of the COXs at 450 nm was 72 (per two flavin adenine dinucleotides), a value similar to that of milk xanthine oxidase and chicken liver xanthine dehydrogenase at 450 nm. That molybdopterin, the novel prosthetic group of the molybdenum cofactor of a variety of molybdoenzymes is also a constituent of COXs from carboxydotrophic bacteria is indicated by the formation of identical fluorescent cofactor derivatives, by complementation of the nitrate reductase activity in extracts of Neurospora crassa nit-1, and by the presence of organic phosphate additional to flavin adenine dinucleotides. Molybdopterin is tightly but noncovalently bound to the protein. COX, sulfite oxidase, xanthine oxidase, and xanthine dehydrogenase each contains 2 mol of molybdopterin per mol of enzyme. The presence of a trichloroacetic acid-releasable, so-far-unidentified, phosphorous-containing moiety in COX is suggested by the resultsmore » of phosphate analysis.« less

Authors:
;
Publication Date:
Research Org.:
Universitaet Goettingen, West Germany
OSTI Identifier:
6265237
Resource Type:
Journal Article
Journal Name:
J. Bacteriol.; (United States)
Additional Journal Information:
Journal Volume: 157:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; OXIDOREDUCTASES; STRUCTURAL CHEMICAL ANALYSIS; PSEUDOMONAS; METABOLISM; CARBON MONOXIDE; MOLYBDENUM; OXIDATION; PHOSPHORUS; BACTERIA; CARBON COMPOUNDS; CARBON OXIDES; CHALCOGENIDES; CHEMICAL REACTIONS; ELEMENTS; ENZYMES; METALS; MICROORGANISMS; NONMETALS; OXIDES; OXYGEN COMPOUNDS; TRANSITION ELEMENTS; 550700* - Microbiology

Citation Formats

Meyer, O, and Rajagopalan, K V. Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria. United States: N. p., 1984. Web.
Meyer, O, & Rajagopalan, K V. Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria. United States.
Meyer, O, and Rajagopalan, K V. 1984. "Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria". United States.
@article{osti_6265237,
title = {Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria},
author = {Meyer, O and Rajagopalan, K V},
abstractNote = {The carbon monoxide oxidases (COXs) purified from the carboxydotrophic bacteria Pseudomonas carboxydohydrogena and Pseudomonas carboxydoflava were found to be molybdenum hydroxylases, identical in cofactor composition and spectral properties to the recently characterized enzyme from Pseudomonas carboxydovorans. All three enzymes exhibited a cofactor composition of two flavin adenine dinucleotides, two molybdenums, eight irons and eight labile sulfides per dimeric molecule, typical for molybdenum-containing iron-sulfur flavoproteins. The millimolar extinction coefficient of the COXs at 450 nm was 72 (per two flavin adenine dinucleotides), a value similar to that of milk xanthine oxidase and chicken liver xanthine dehydrogenase at 450 nm. That molybdopterin, the novel prosthetic group of the molybdenum cofactor of a variety of molybdoenzymes is also a constituent of COXs from carboxydotrophic bacteria is indicated by the formation of identical fluorescent cofactor derivatives, by complementation of the nitrate reductase activity in extracts of Neurospora crassa nit-1, and by the presence of organic phosphate additional to flavin adenine dinucleotides. Molybdopterin is tightly but noncovalently bound to the protein. COX, sulfite oxidase, xanthine oxidase, and xanthine dehydrogenase each contains 2 mol of molybdopterin per mol of enzyme. The presence of a trichloroacetic acid-releasable, so-far-unidentified, phosphorous-containing moiety in COX is suggested by the results of phosphate analysis.},
doi = {},
url = {https://www.osti.gov/biblio/6265237}, journal = {J. Bacteriol.; (United States)},
number = ,
volume = 157:2,
place = {United States},
year = {Wed Feb 01 00:00:00 EST 1984},
month = {Wed Feb 01 00:00:00 EST 1984}
}