X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima - PubMed (original) (raw)

. 2008 Jul 4;283(27):18861-72.

doi: 10.1074/jbc.M801161200. Epub 2008 Apr 8.

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X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima

Yvain Nicolet et al. J Biol Chem. 2008.

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Abstract

Maturation of the [FeFe]-hydrogenase active site depends on at least the expression of three gene products called HydE, HydF, and HydG. We have solved the high resolution structure of recombinant, reconstituted S-adenosine-L-methionine-dependent HydE from Thermotoga maritima. Besides the conserved [Fe(4)S(4)] cluster involved in the radical-based reaction, this HydE was reported to have a second [Fe(4)S(4)] cluster coordinated by three Cys residues. However, in our crystals, depending on the reconstitution and soaking conditions, this second cluster is either a [Fe(2)S(2)] center, with water occupying the fourth ligand site or is absent. We have carried out site-directed mutagenesis studies on the related HydE from Clostridium acetobutylicum, along with in silico docking and crystal soaking experiments, to define the active site region and three anion-binding sites inside a large, positive cavity, one of which binds SCN(-) with high affinity. Although the overall triose-phosphate isomerase-barrel structure of HydE is very similar to that of biotin synthase, the residues that line the internal cavity are significantly different in the two enzymes.

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