Aug 11, 2011

Insights into [FeFe]-hydrogenase structure, mechanism, and maturation

David W MulderJohn W Peters


Hydrogenases are metalloenzymes that are key to energy metabolism in a variety of microbial communities. Divided into three classes based on their metal content, the [Fe]-, [FeFe]-, and [NiFe]-hydrogenases are evolutionarily unrelated but share similar nonprotein ligand assemblies at their active site metal centers that are not observed elsewhere in biology. These nonprotein ligands are critical in tuning enzyme reactivity, and their synthesis and incorporation into the active site clusters require a number of specific maturation enzymes. The wealth of structural information on different classes and different states of hydrogenase enzymes, biosynthetic intermediates, and maturation enzymes has contributed significantly to understanding the biochemistry of hydrogen metabolism. This review highlights the unique structural features of hydrogenases and emphasizes the recent biochemical and structural work that has created a clearer picture of the [FeFe]-hydrogenase maturation pathway.

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Mentioned in this Paper

Biochemical Pathway
Calabaria reinhardtii
Covalent Interaction
Bacterial Proteins
Clostridium pasteurianum
Carboxy-Terminal Amino Acid
Post-Translational Protein Processing

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