Work

Properties of a thermostable 4Fe-ferredoxin from the hyperthermophilic bacterium Thermotoga maritima

Year: 1994

Type: article

Abstract: A ferredoxin has been purified from one of the most ancient and most thermophilic bacteria known, Thermotoga maritima, which grows up to 90 degrees C. The reduced protein (M(r) approx. 6300) contains a single S = 1/2 [4Fe-4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95 degrees C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.

Source: FEMS Microbiology Letters

DOI: 10.1016/0378-1097(94)90122-8

Authors: Jenny M. Blamey, Swarnalatha Mukund, Michael W.W. Adams

Institution: University of Georgia

Language: English

Topic: Metalloenzymes and iron-sulfur proteins

Subfield: Renewable Energy, Sustainability and the Environment

Field: Energy

Domain: Physical Sciences

Open Access status: bronze

Funders: National Science Foundation, U.S. Department of Energy

Award: G3798569771