Hydrogen　is　a　promising　clean　energy　resource.　However,　the　biohydrogen　production　efficiency　needs　to　be　significantly　improved　to　make　it　competitive　to　fossil　fuels.　Formate　dehydrogenase,　which　is　a　catalyst　in　the　production　of　2H+,　2e-,　and　CO2　from　formate,　is　a　critical　enzyme　in　hydrogen　production　by　bacteria.　In　this　study　the　formate　dehydrogenase　(fdhF)　gene　from　Bacillus　cereus　strain　XN12　was　cloned.　The　sequencing　analysis　revealed　that　the　cloned　fdhF　gene　contained　2937base　pairs,　39.3%　GC　content　and　shared　100%　identity　with　the　fdhF　gene　of　Bacillus　cereus　strain　Q1　(genebank　No.　CP000227.1).　To　characterize　the　fdhF　gene　product　of　Bacillus　cereus　strain　XN12,　the　fdhF　gene　was　then　subcloned　into　pET32a　and　the　resulting　pET32-FDHF-His　plasmid　was　transformed　into　Escherichia　coli　BL21　cells.　Through　the　IPTG　induction,　the　cloned　fdhF　gene　was　efficiently　overexpressed.　The　recombinant　FdhF　protein　was　highly　functional　as　demonstrated　by　BV　reduction　experiment.　It　was　found　that　the　hydrogen　production　rate　of　recombinant　FdhF　protein　was　greatly　influenced　by　the　presence　of　various　metal　ions,　among　which　MoO42-　and　SeO32-　increased　the　hydrogen　production　mainly　by　increase　recombinant　protein　expression.　The　hydrogen　production　was　also　higher　when　glucose　used　as　the　substrate　than　formate　used　as　the　substrate.　The　results　suggested　that　recombinant　Bacillus　cereus　formate　dehydrogenase　protein　was　a　promising　solution　for　improving　biohydrogen　production.　©　2018,　Editorial　Board　of　China　Environmental　Science.　All　right　reserved.