The Oxidation of Nicotinic Acid by Pseudomonas Ovalis Chester. The Terminal Oxidase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1972 Sep 1

PMID 4349118

Citations 7

Authors

M V Jones

D E Hughes

Affiliations

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Abstract

In cell-free extracts of Pseudomonas ovalis nicotinic acid oxidase is confined to the wallmembrane fraction. It is associated with an electron-transport chain comprising b- and c-type cytochromes only, differing proportions of which are reduced by nicotinate and NADH. CO difference-spectra show two CO-binding pigments, cytochrome o (absorption maximum at 417nm) and another component absorbing maximally at 425nm. Cytochrome o is not reduced by NADH or by succinate but is by nicotinate, which can also reduce the ;425' CO-binding pigment. The effects of inhibitors of terminal oxidation support the idea of two terminal oxidases and a scheme involving the ;425' CO-binding pigment and the other components of the electron-transport chain is proposed.

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References

Hunt A . Purification of the nicotinic acid hydroxylase system of Pseudomonas fluorescens KB1. Biochem J. 1959; 72(1):1-7. PMC: 1196872. DOI: 10.1042/bj0720001. View

Plesnicar M, BONNER Jr W, Storey B . Peroxidase associated with higher plant mitochondria. Plant Physiol. 1967; 42(3):366-70. PMC: 1086543. DOI: 10.1104/pp.42.3.366. View

Peterson J . Cytochrome content of two pseudomonads containing mixed-function oxidase systems. J Bacteriol. 1970; 103(3):714-21. PMC: 248149. DOI: 10.1128/jb.103.3.714-721.1970. View

Jones C, REDFEARN E . The cytochrome system of Azotobacter vinelandii. Biochim Biophys Acta. 1967; 143(2):340-53. DOI: 10.1016/0005-2728(67)90088-6. View

Eady R, Jarman T, Large P . Microbial oxidation of amines. Partial purification of a mixed-function secondary-amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome-P-420-type haemoprotein. Biochem J. 1971; 125(2):449-59. PMC: 1178079. DOI: 10.1042/bj1250449. View

ELLFOLK N, Soininen R . Pseudomonas cytochrome c peroxidase. I. Purification procedure. Acta Chem Scand. 1970; 24(6):2126-36. DOI: 10.3891/acta.chem.scand.24-2126. View

ORNSTON L . Regulation of catabolic pathways in Pseudomonas. Bacteriol Rev. 1971; 35(2):87-116. PMC: 378377. DOI: 10.1128/br.35.2.87-116.1971. View

Daniel R . The electron transport system of Acetobacter suboxydans with particular reference to cytochrome. Biochim Biophys Acta. 1970; 216(2):328-41. DOI: 10.1016/0005-2728(70)90224-0. View

Hunt A, Hughes D, Lowenstein J . The hydroxylation of nicotinic acid by Pseudomonas fluorescens. Biochem J. 1958; 69(2):170-3. PMC: 1196534. DOI: 10.1042/bj0690170. View

10.

Hughes D . 6-Hydroxynicotinic acid as an intermediate in the oxidation of nicotinic acid by Pseudomonas fluorescens. Biochem J. 1955; 60(2):303-10. PMC: 1215697. DOI: 10.1042/bj0600303. View

11.

Hughes D . A press for disrupting bacteria and other micro-organisms. Br J Exp Pathol. 1951; 32(2):97-109. PMC: 2073399. View

12.

Behrman E, STANIER R . The bacterial oxidation of nicotinic acid. J Biol Chem. 1957; 228(2):923-45. View

13.

Lenhoff H, Kaplan N . A cytochrome peroxidase from Pseudomonas fluorescens. J Biol Chem. 1956; 220(2):967-82. View

14.

Francis M, Hughes D, Kornberg H, PHIZACKERLEY P . THE OXIDATION OF L-MALATE BY PSEUDOMONAS SP. Biochem J. 1963; 89:430-8. PMC: 1202447. DOI: 10.1042/bj0890430. View

15.

Oka T, Arima K . Cyanide Resistance in Achromobacter II. Mechanism of Cyanide Resistance. J Bacteriol. 1965; 90(3):744-7. PMC: 369635. DOI: 10.1128/jb.90.3.744-747.1965. View

16.

LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

17.

Katagiri M, Ganguli B, GUNSALUS I . A soluble cytochrome P-450 functional in methylene hydroxylation. J Biol Chem. 1968; 243(12):3543-6. View

18.

Chance B, Williams G . Respiratory enzymes in oxidative phosphorylation. III. The steady state. J Biol Chem. 1955; 217(1):409-27. View