Oxygen consumption by Desulfovibrio strains with and without polyglucose
(1998) In Applied and Environmental Microbiology 64(3). p.1034-1039- Abstract
- The kinetics of oxygen reduction by Desulfovibrio salexigens Mast1 and the role of polyglucose in this activity were examined and compared with those of strains of D. desulfuricans and D. gigas. Oxidation rates were highest at air saturation (up to 40 nmol of O2min−1 mg of protein−1) and declined with decreasing oxygen concentrations. Studies with cell extracts (CE) indicated that NADH oxidase was entirely responsible for the oxygen reduction in strain Mast1. In D. desulfuricans CSN, at least three independent systems appeared to reduce oxygen. Two were active at all oxygen concentrations (NADH oxidase and NADPH oxidase), and one was maximally active at less than 10 μM oxygen. In contrast to D. gigas and D. salexigens strains, theD.... (More)
- The kinetics of oxygen reduction by Desulfovibrio salexigens Mast1 and the role of polyglucose in this activity were examined and compared with those of strains of D. desulfuricans and D. gigas. Oxidation rates were highest at air saturation (up to 40 nmol of O2min−1 mg of protein−1) and declined with decreasing oxygen concentrations. Studies with cell extracts (CE) indicated that NADH oxidase was entirely responsible for the oxygen reduction in strain Mast1. In D. desulfuricans CSN, at least three independent systems appeared to reduce oxygen. Two were active at all oxygen concentrations (NADH oxidase and NADPH oxidase), and one was maximally active at less than 10 μM oxygen. In contrast to D. gigas and D. salexigens strains, theD. desulfuricans strains also contained NADH peroxidase and NADPH peroxidase activities and did not accumulate polyglucose under nonlimiting growth conditions. At air saturation, initial activities of the oxidases and peroxidases of cells harvested at the end of the log phase were on the order of 20 to 140 nmol of O2min−1 mg of protein−1. In all strains, these enzymes were relatively stable but were susceptible to inactivation as soon as substrates were added to the assay mixture. Under those conditions, all oxidation activity disappeared after ca. 1 h of incubation. The same finding was observed with whole cells of D. desulfuricans CSN and D. desulfuricans ATCC 27774, but inactivation was less pronounced with cells of D. salexigens Mast1. It appeared that the presence of polyglucose in the whole cells retarded the process of inactivation of NADH oxidase, but this property was lost in crude CE. In spite of the effect of polyglucose on the oxidative potential, oxygen-dependent growth of D. salexigens Mast1 could be demonstrated neither in batch nor in continuous culture. (Less)
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- author
- van Niel, Ed LU and Gottschal, JC
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- keywords
- sulfate reduction, polyglucose, oxygen metabolism, Desulfovibrio salexigens, Desulfovibrio desulfuricans, Desulfovibrio gigas
- in
- Applied and Environmental Microbiology
- volume
- 64
- issue
- 3
- pages
- 6 pages
- publisher
- American Society for Microbiology
- external identifiers
-
- scopus:0031909736
- ISSN
- 0099-2240
- language
- English
- LU publication?
- no
- id
- 7aa8e39d-b1cd-4b2a-b669-9264a809d201
- date added to LUP
- 2016-09-16 16:26:45
- date last changed
- 2022-01-30 06:02:53
@article{7aa8e39d-b1cd-4b2a-b669-9264a809d201,
abstract = {{The kinetics of oxygen reduction by Desulfovibrio salexigens Mast1 and the role of polyglucose in this activity were examined and compared with those of strains of D. desulfuricans and D. gigas. Oxidation rates were highest at air saturation (up to 40 nmol of O2min−1 mg of protein−1) and declined with decreasing oxygen concentrations. Studies with cell extracts (CE) indicated that NADH oxidase was entirely responsible for the oxygen reduction in strain Mast1. In D. desulfuricans CSN, at least three independent systems appeared to reduce oxygen. Two were active at all oxygen concentrations (NADH oxidase and NADPH oxidase), and one was maximally active at less than 10 μM oxygen. In contrast to D. gigas and D. salexigens strains, theD. desulfuricans strains also contained NADH peroxidase and NADPH peroxidase activities and did not accumulate polyglucose under nonlimiting growth conditions. At air saturation, initial activities of the oxidases and peroxidases of cells harvested at the end of the log phase were on the order of 20 to 140 nmol of O2min−1 mg of protein−1. In all strains, these enzymes were relatively stable but were susceptible to inactivation as soon as substrates were added to the assay mixture. Under those conditions, all oxidation activity disappeared after ca. 1 h of incubation. The same finding was observed with whole cells of D. desulfuricans CSN and D. desulfuricans ATCC 27774, but inactivation was less pronounced with cells of D. salexigens Mast1. It appeared that the presence of polyglucose in the whole cells retarded the process of inactivation of NADH oxidase, but this property was lost in crude CE. In spite of the effect of polyglucose on the oxidative potential, oxygen-dependent growth of D. salexigens Mast1 could be demonstrated neither in batch nor in continuous culture.}},
author = {{van Niel, Ed and Gottschal, JC}},
issn = {{0099-2240}},
keywords = {{sulfate reduction; polyglucose; oxygen metabolism; Desulfovibrio salexigens; Desulfovibrio desulfuricans; Desulfovibrio gigas}},
language = {{eng}},
number = {{3}},
pages = {{1034--1039}},
publisher = {{American Society for Microbiology}},
series = {{Applied and Environmental Microbiology}},
title = {{Oxygen consumption by Desulfovibrio strains with and without polyglucose}},
url = {{https://lup.lub.lu.se/search/files/12292797/VanNielGotschal1998.pdf}},
volume = {{64}},
year = {{1998}},
}