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Journal Article

Cytochrome c-dependent methacrylate reductase from Geobacter sulfurreducens AM-1

MPS-Authors

Mikoulinskaia,  Oxana
external;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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Thauer,  Rudolf K.       
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

Hedderich,  Reiner
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

External Resource

https://doi.org/10.1046/j.1432-1327.1999.00489.x
(Publisher version)

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Citation

Mikoulinskaia, O., Akimenko, V., Galouchko, A., Thauer, R. K., & Hedderich, R. (1999). Cytochrome c-dependent methacrylate reductase from Geobacter sulfurreducens AM-1. European Journal of Biochemistry, 263(2), 346-352. doi:10.1046/j.1432-1327.1999.00489.x.


Cite as: https://hdl.handle.net/21.11116/0000-000F-ADDE-5
Abstract
Geobacter sulfurreducens AM-1 can use methacrylate as a terminal electron acceptor for anaerobic respiration. In this paper, we report on the purification and properties of the periplasmic methacrylate reductase, and show that the enzyme is dependent on the presence of a periplasmic cytochrome c (apparent K-m = 0.12 mu M). The methacrylate reductase was found to be composed of only one polypeptide with an apparent molecular mass of 50 kDa and to contain, bound tightly but not covalently, 1 mol of FAD per mel. The N-terminal, amino acid sequence showed sequence similarity to a periplasmic fumarate reductase from Shewanella putrefaciens. However, methacrylate reductase did not catalyze the reduction of fumarate. The periplasmic cytochrome c, which was also purified, had an apparent molecular mass of 30 kDa and contained approximate to 4 mol of heme mol(-1). Cells of G. sulfurreducens AM-1 grown on acetate and methacrylate as; an energy source were found to contain all the enzymes required for the oxidation of acetate to CO2 via the citric acid cycle.