Electron transfer coupled to Mn(II) oxidation in two deep-sea Pacific Ocean isolates
Abstract
Recent work conducted to elucidate the electron transport pathway involved in Mn(II)-oxidation by Oceanospirillum strains BIII 45 and BIII 82 was reviewed and new information concerned with the cellular organization of the Mn(II)-oxidoreductase system in these organisms was presented. The presence of both b-type and c-type cytochromes was found in both strains. Cytochromes found were predominantly assoiated with the membrane fraction. A small amount was found in the periplasmic fraction. No cytochromes were found in the intracellular fraction. Mn(II) was able to reduce the c-type cytochrome only when membranes were combined with either periplasmic or intracellular fractions. An hypothesis for the mechanism of Mn(II) oxidation (similar to FeII oxidation) is presented. In this mechanism, rusticyanin is the primary electron acceptor. The oxidized rusticyanin then reduces a c-type cytochrome in the periplasmic space. The reduced cytochrome c then reduces a membrane a-type cytochrome oxidase. This would explain the necessity of combining fractions to obtain cytochrome reduction on Mn(II) addition.
- Authors:
- Publication Date:
- Research Org.:
- Oak Ridge National Lab., TN (USA); Rensselaer Polytechnic Inst., Troy, NY (USA)
- OSTI Identifier:
- 5826030
- Report Number(s):
- CONF-790858-1
- DOE Contract Number:
- W-7405-ENG-26
- Resource Type:
- Conference
- Resource Relation:
- Conference: 4. international symposium on environmental biogeochemistry, Canberra, Australia, 27 Aug 1979
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; ELECTRON TRANSFER; BIOLOGICAL PATHWAYS; OXIDOREDUCTASES; BIOCHEMICAL REACTION KINETICS; BACTERIA; CELL MEMBRANES; CYTOCHROME OXIDASE; CYTOCHROMES; MANGANESE; OXIDATION; CELL CONSTITUENTS; CHEMICAL REACTIONS; ELEMENTS; ENZYMES; KINETICS; MEMBRANES; METALS; MICROORGANISMS; OXIDASES; PIGMENTS; REACTION KINETICS; TRANSITION ELEMENTS; 550200* - Biochemistry
Citation Formats
Arcuri, E. J., and Ehrlich, H. L. Electron transfer coupled to Mn(II) oxidation in two deep-sea Pacific Ocean isolates. United States: N. p., 1979.
Web.
Arcuri, E. J., & Ehrlich, H. L. Electron transfer coupled to Mn(II) oxidation in two deep-sea Pacific Ocean isolates. United States.
Arcuri, E. J., and Ehrlich, H. L. 1979.
"Electron transfer coupled to Mn(II) oxidation in two deep-sea Pacific Ocean isolates". United States. https://www.osti.gov/servlets/purl/5826030.
@article{osti_5826030,
title = {Electron transfer coupled to Mn(II) oxidation in two deep-sea Pacific Ocean isolates},
author = {Arcuri, E. J. and Ehrlich, H. L.},
abstractNote = {Recent work conducted to elucidate the electron transport pathway involved in Mn(II)-oxidation by Oceanospirillum strains BIII 45 and BIII 82 was reviewed and new information concerned with the cellular organization of the Mn(II)-oxidoreductase system in these organisms was presented. The presence of both b-type and c-type cytochromes was found in both strains. Cytochromes found were predominantly assoiated with the membrane fraction. A small amount was found in the periplasmic fraction. No cytochromes were found in the intracellular fraction. Mn(II) was able to reduce the c-type cytochrome only when membranes were combined with either periplasmic or intracellular fractions. An hypothesis for the mechanism of Mn(II) oxidation (similar to FeII oxidation) is presented. In this mechanism, rusticyanin is the primary electron acceptor. The oxidized rusticyanin then reduces a c-type cytochrome in the periplasmic space. The reduced cytochrome c then reduces a membrane a-type cytochrome oxidase. This would explain the necessity of combining fractions to obtain cytochrome reduction on Mn(II) addition.},
doi = {},
url = {https://www.osti.gov/biblio/5826030},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 1979},
month = {Mon Jan 01 00:00:00 EST 1979}
}