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Biochemistry of Catabolic Reductive Dehalogenation
Maeva Fincker1, Alfred M Spormann1
1Department of Civil and Environmental Engineering and Department of Chemical Engineering, Stanford University, Stanford, California 94305; email: mfincker@stanford.edu , spormann@stanford.edu.
Annual Review of Biochemistry
|June 28, 2017
Summary
Microorganisms conserve energy by breaking down organohalides using reductive dehalogenases. This review details these enzymes, their electron transfer chains, and distinct energy conservation strategies.
Area of Science:
- Biochemistry
- Microbiology
- Environmental Science
Background:
- Diverse microorganisms perform reductive dehalogenation of organohalides for energy.
- Key enzymes are membrane-associated, corrinoid and Fe-S cluster-containing reductive dehalogenases.
- These enzymes act as terminal reductases in short electron transfer chains.
Purpose of the Study:
- To review current knowledge on catabolic reductive dehalogenases.
- To discuss the electron transfer chains involved in reductive dehalogenation.
- To explore reaction mechanisms, cofactor roles, and physiological implications.
Main Methods:
- Enzymatic studies of reductive dehalogenases.
- Physiological studies of microorganisms utilizing reductive dehalogenation.
- Comparative analysis of enzyme structures and functions.
Main Results:
- Identified quinone-dependent and quinone-independent reductive dehalogenases.
- Distinguished enzyme types based on amino acid sequences.
- Implied different energy conservation mechanisms linked to enzyme types.
Conclusions:
- Reductive dehalogenases are crucial for organohalide metabolism and energy conservation.
- Enzyme diversity suggests varied bioenergetic strategies in microorganisms.
- Further research on mechanisms and cofactors is warranted.
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