HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Doughty, D. M. Articles by Bottomley, P. J. Search for Related Content PubMed PubMed Citation Articles by Doughty, D. M. Articles by Bottomley, P. J. Agricola Articles by Doughty, D. M. Articles by Bottomley, P. J.

Propionate inactivation of butane monooxygenase activity in ‘Pseudomonas butanovora’: biochemical and physiological implications

¹ Department of Microbiology, Oregon State University, Corvallis, OR 97331-3804, USA
² Program of Molecular and Cellular Biology, Oregon State University, Corvallis, OR 97331-3804, USA
³ Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR 97331-3804, USA
⁴ Department of Crop and Soil Science, Oregon State University, Corvallis, OR 97331-3804, USA

Correspondence
Peter J. Bottomley
Peter.Bottomley{at}oregonstate.edu

Butane monooxygenase (BMO) catalyses the oxidation of alkanes to alcohols in the alkane-utilizing bacterium ‘Pseudomonas butanovora’. Incubation of alkane-grown ‘P. butanovora’ with butyrate or propionate led to irreversible time- and O₂-dependent loss of BMO activity. In contrast, BMO activity was unaffected by incubation with lactate or acetate. Chloramphenicol inhibited the synthesis of new BMO, but did not change the kinetics of propionate-dependent BMO inactivation, suggesting that the propionate effect was not simply due to it acting as a repressor of BMO transcription. BMO was protected from propionate-dependent inactivation by the presence of its natural substrate, butane. Although both the time and O₂ dependency of propionate inactivation of BMO imply that propionate might be a suicide substrate, no evidence was obtained for BMO-dependent propionate consumption, or ¹⁴C labelling of BMO polypeptides by [2-¹⁴C]propionate during inactivation. Propionate-dependent BMO inactivation was also explored in mutant strains of ‘P. butanovora’ containing single amino acid substitutions in the -subunit of the BMO hydroxylase. Propionate-dependent BMO inactivation in two mutant strains with amino acid substitutions close to the catalytic site differed from wild-type (one was more sensitive and the other less), providing further evidence that propionate-dependent inactivation involves interaction with the BMO catalytic site. A putative model is presented that might explain propionate-dependent inactivation of BMO when framed within the context of the catalytic cycle of the closely related enzyme, soluble methane monooxygenase.

This article has been cited by other articles:

				R. B. Cooley, B. L. Dubbels, L. A. Sayavedra-Soto, P. J. Bottomley, and D. J. Arp Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly 'Pseudomonas butanovora' Microbiology, June 1, 2009; 155(6): 2086 - 2096. [Abstract] [Full Text] [PDF]

				D. M. Doughty, E. G. Kurth, L. A. Sayavedra-Soto, D. J. Arp, and P. J. Bottomley Evidence for Involvement of Copper Ions and Redox State in Regulation of Butane Monooxygenase in Pseudomonas butanovora J. Bacteriol., April 15, 2008; 190(8): 2933 - 2938. [Abstract] [Full Text] [PDF]

				E. G. Kurth, D. M. Doughty, P. J. Bottomley, D. J. Arp, and L. A. Sayavedra-Soto Involvement of BmoR and BmoG in n-alkane metabolism in 'Pseudomonas butanovora' Microbiology, January 1, 2008; 154(1): 139 - 147. [Abstract] [Full Text] [PDF]