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- W2084849130 abstract "The [FeFe]-hydrogenase of Rhodospirillum rubrum (Rr-HydA; Rru_A0310) was expressed in an Escherichia coli strain co-expressing the hydrogenase maturation proteins HydE, HydF, and HydG from Clostridium acetobutylicum (Ca-HydEFG). Rr-HydA, which purified as a 50 kDa protein, showed an in vitro H2-evolving activity in the presence of dithionite-reduced methyl viologen. The ability of Rr-HydA to carry out H2-evolving activity when heterologously expressed in a Rhodobacter sphaeroides nifDK hupSL mutant containing the genes coding for Ca-HydEFG was examined. Photoheterotrophic H2 evolution was only observed in the presence of Rr-HydB [Rru_A0309 (22 kDa)], which is encoded by a gene located immediately upstream from the gene encoding Rr-HydA. Rr-HydB contains Fe–S cluster(s). Consistently, in a reaction mixture containing spinach ferredoxin oxidoreductase and NADPH, H2 was evolved when both Rr-HydA and Rr-HydB were present together, and the rate of H2 evolution by Rr-HydA was proportional to the level of Rr-HydB until an equimolar ratio of the two proteins was reached. Thus, it is proposed that Rr-HydB acts as Rr-HydA-specific ferredoxin that donates electrons to Rr-HydA through a direct molecular interaction." @default.
- W2084849130 created "2016-06-24" @default.
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- W2084849130 date "2015-04-01" @default.
- W2084849130 modified "2023-09-25" @default.
- W2084849130 title "The ferredoxin Rr-HydB is required for the H2-evolving activity of Rr-HydA, a [FeFe]-hydrogenase of Rhodospirillum rubrum" @default.
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- W2084849130 doi "https://doi.org/10.1016/j.ijhydene.2015.01.173" @default.
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