Biochemistry of Catabolic Reductive Dehalogenation.

Maeva Fincker, Alfred M Spormann

Journal: Annual review of biochemistry 2017;86():357-386

PMID: 28654328

Abstract

A wide range of phylogenetically diverse microorganisms couple the reductive dehalogenation of organohalides to energy conservation. Key enzymes of such anaerobic catabolic pathways are corrinoid and Fe-S cluster-containing, membrane-associated reductive dehalogenases. These enzymes catalyze the reductive elimination of a halide and constitute the terminal reductases of a short electron transfer chain. Enzymatic and physiological studies revealed the existence of quinone-dependent and quinone-independent reductive dehalogenases that are distinguishable at the amino acid sequence level, implying different modes of energy conservation in the respective microorganisms. In this review, we summarize current knowledge about catabolic reductive dehalogenases and the electron transfer chain they are part of. We review reaction mechanisms and the role of the corrinoid and Fe-S cluster cofactors and discuss physiological implications.

Address: Department of Civil and Environmental Engineering and Department of Chemical Engineering, Stanford University, Stanford, California 94305; email: [email protected] , [email protected].

DOI: 10.1146/annurev-biochem-061516-044829

Link outs

Free resources

Other Literature Sources:

https://scite.ai/reports/28654328

Miscellaneous:

https://assays.cancer.gov/CPTAC-1778

Subscription / membership required

Full Text Sources:

https://www.annualreviews.org/content/journals/10....

MeSH Terms: Amino Acid Sequence, Bacterial Proteins, Benzoquinones, Biocatalysis, Chloroflexi, Coenzymes, Corrinoids, Electron Transport, Energy Metabolism, Gene Expression, Halogens, Kinetics, Models, Molecular, Oxidoreductases, Phylogeny, Substrate Specificity, Vitamin B 12