HydF as a scaffold protein in [FeFe] hydrogenase H-cluster biosynthesis |
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| Authors: | McGlynn Shawn E Shepard Eric M Winslow Mark A Naumov Anatoli V Duschene Kaitlin S Posewitz Matthew C Broderick William E Broderick Joan B Peters John W |
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| Institution: | Department of Chemistry and Biochemistry, The Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, USA. |
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| Abstract: | In an effort to determine the specific protein component(s) responsible for in vitro activation of the FeFe] hydrogenase (HydA), the individual maturation proteins HydE, HydF, and HydG from Clostridium acetobutylicum were purified from heterologous expressions in Escherichia coli. Our results demonstrate that HydF isolated from a strain expressing all three maturation proteins is sufficient to confer hydrogenase activity to purified inactive heterologously expressed HydA (expressed in the absence of HydE, HydF, and HydG). These results represent the first in vitro maturation of FeFe] hydrogenase with purified proteins, and suggest that HydF functions as a scaffold upon which an H-cluster intermediate is synthesized. |
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| Keywords: | HydAΔEFG HydA expressed in the absence of HydE HydF and HydG HydFEG HydF co-expressed with HydE and HydG HydFΔEG HydF expressed in the absence of HydE and HydG AdoMet S-adenosylmethionine |
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