AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Trimble, R. B.
Right arrow Articles by Ehrlich, H. L.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Trimble, R. B.
Right arrow Articles by Ehrlich, H. L.
Agricola
Right arrow Articles by Trimble, R. B.
Right arrow Articles by Ehrlich, H. L.

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1970 June; 19(6): 966-972
Copyright © 1970 American Society for Microbiology. All Rights Reserved.

Bacteriology of Manganese Nodules

IV. Induction of an MnO2-Reductase System in a Marine Bacillus1

R. B. Trimble2 and H. L. Ehrlich

Department of Biology, Rensselaer Polytechnic Institute, Troy, New York 12181

ABSTRACT

Bacillus 29, isolated from a ferromanganese nodule from the Atlantic Ocean, was shown to possess an MnO2-reductase system which is induced in the presence of manganous ion. Maximal activity of the enzyme system was induced in about 5 hr in the presence of 4.35 mM MnSO4 and was minimally dependent on the presence of either glucose or peptone and oxygen. Induction of optimal activity required the simultaneous presence of glucose and peptone. At least 30% of maximal activity was induced in 5 hr in the presence of 0.4 µM MnSO4. Actinomycin D (5 µg/ml) or chloramphenicol (35 µg/ml), when added to the induction medium, inhibited approximately 90% of MnO2-reductase synthesis and incorporation of uracil-2-14C or leucine-1-14C. Cell-free extracts having MnO2-reductase activity were prepared by sonic disruption of cell suspensions of induced Bacillus 29. Such extracts used glucose metabolism as a source of electrons. They had an average specific activity of 1.15 nmoles of MnII produced per mg of protein per hr at 25 C. They had a temperature optimum of 18 C for reductase activity and retained 50% of their activity at 4 C, the approximate temperature of the natural habitat of the organism. Extracts were stable for several days at 4 C but rapidly lost over 50% of their activity on freezing and thawing. Over 90% of the activity of the extract could be destroyed by heating in a boiling-water bath for 5 min. At a concentration of 1 mM, HgCl2 and atebrine dihydrochloride inhibited MnO2-reductase activity by at least 50%, but sodium azide was ineffective. The MnO2-reductase activity of induced cells and extracts from them was no greater in the absence of oxygen than in its presence, confirming an earlier observation that MnO2 and O2 do not compete as terminal electron acceptors in the respiratory activity of this organism.


FOOTNOTES

2 Present address: Division of Laboratories and Research, New York State Department of Health, Albany, N. Y. 12201.

1 Part of a dissertation submitted by the senior author to the Department of Biology of Rensselaer Polytechnic Institute in partial fulfillment of the requirements for the Ph.D. degree.


Appl Environ Microbiol. 1970 June; 19(6): 966-972
Copyright © 1970 American Society for Microbiology. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 1970 by the American Society for Microbiology. All rights reserved.