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A Universal Scaffold for Synthesis of the Fe(CN)(2)(CO) Moiety of [NiFe] Hydrogenase
Zitatschlüssel ISI:000310982800041
Autor Buerstel, Ingmar and Siebert, Elisabeth and Winter, Gordon and Hummel, Philipp and Zebger, Ingo and Friedrich, Baerbel and Lenz, Oliver
Seiten 38845-38853
Jahr 2012
ISSN 0021-9258
DOI 10.1074/jbc.M112.376947
Adresse 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
Journal JOURNAL OF BIOLOGICAL CHEMISTRY
Jahrgang 287
Nummer 46
Monat NOV 9
Verlag AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Zusammenfassung Hydrogen-cycling [NiFe] hydrogenases harbor a dinuclear catalytic center composed of nickel and iron ions, which are coordinated by four cysteine residues. Three unusual diatomic ligands in the form of two cyanides (CN-) and one carbon monoxide (CO) are bound to the iron and apparently account for the complexity of the cofactor assembly process, which involves the function of at least six auxiliary proteins, designated HypA, -B, -C, -D, -E, and -F. It has been demonstrated previously that the HypC, -D, -E, and -F proteins participate in cyanide synthesis and transfer. Here, we show by infrared spectroscopic analysis that the purified HypCD complexes from Ralstonia eutropha and Escherichia coli carry in addition to both cyanides the CO ligand. We present experimental evidence that in vivo the attachment of the CN- ligands is a prerequisite for subsequent CO binding. With the aid of genetic engineering and subsequent mutant analysis, the functional role of conserved cysteine residues in HypD from R. eutropha was investigated. Our results demonstrate that the HypCD complex serves as a scaffold for the assembly of the Fe(CN)(2)(CO) entity of [NiFe] hydrogenase.
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