Tritrichomonas foetus and Trichomonas vaginalis: the pattern of inactivation of hydrogenase activity by oxygen and activities of catalase and ascorbate peroxidase

1 Author for correspondence: Geoffrey D. Smith. Tel: +61 6 249 2843. Fax: +61 6 249 0313. e-mail: Geoffrey.Smith@anu.edu.au Division of Biochemistry and Molecular Biology, School of Life Sciences, Faculty of Science, The Australian National University, Canberra, ACT 0200, Australia ABSTRACT The conc...

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Published inMicrobiology (Society for General Microbiology) Vol. 142; no. 1; pp. 207 - 211
Main Authors Page-Sharp, Madhu, Behm, Carolyn A, Smith, Geoffrey D
Format Journal Article
LanguageEnglish
Published Reading Soc General Microbiol 01.01.1996
Society for General Microbiology
Subjects
Animals
Ascorbate Peroxidases
Biochemistry. Physiology. Immunology. Molecular biology
Biological and medical sciences
Catalase - analysis
Fundamental and applied biological sciences. Psychology
Hydrogen - metabolism
Hydrogenase - drug effects
Oxygen - pharmacology
Peroxidases - analysis
Protozoa
Trichomonas vaginalis
Trichomonas vaginalis - enzymology
Tritrichomonas foetus
Tritrichomonas foetus - enzymology
Trichomonas vaginalis
Protozoa
Oxygen
Enzyme
L-Ascorbate peroxidase
Trichomonadida
Metabolism
Tritrichomonas foetus
Hydrogenase
Peroxidases
Enzymatic activity
Catalase
Oxidoreductases
Kinetic parameter
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Summary:1 Author for correspondence: Geoffrey D. Smith. Tel: +61 6 249 2843. Fax: +61 6 249 0313. e-mail: Geoffrey.Smith@anu.edu.au Division of Biochemistry and Molecular Biology, School of Life Sciences, Faculty of Science, The Australian National University, Canberra, ACT 0200, Australia ABSTRACT The concentration-dependence of the inhibition of whole-cell hydrogen formation by oxygen has been measured in the trichomonads Trichomonas vaginalis and Tritrichomonas foetus, and compared with the oxygen inhibition of the in situ hydrogenase activity as measured by a tritium exchange assay. The inhibition profiles closely paralleled each other, suggesting that hydrogenase is the primary site of inhibition of anaerobic fermentative metabolism. In addition the inhibition profile for isolated hydrogenosomes was measured and shown to be similar to that for whole organisms. Ascorbate peroxidase was shown to be present in both organisms whereas catalase was confirmed to be present only in Tritr. foetus. The kinetic parameters of both enzymes were measured and their respective roles in oxygen protection discussed. Keywords: Tritrichomonas foetus, , Trichomonas vaginalis, , hydrogenase, catalase, ascorbate peroxidase
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1350-0872
1465-2080
DOI:10.1099/13500872-142-1-207