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replacements at the H2-activating site of the NAD-reducing hydrogenase from Alcaligenes eutrophus. Biochemistry 1999,38(43):14330–14337.CrossRefPubMed Authors’ contributions ED performed most experimental work; Most of the transcriptional studies of hupW and hoxW, all studies done in silico including phylogenetic studies and specificity studies and analysis of the data. She is the primary author of the final manuscript. MH identified the TSPs of alr1422/hupW in Nostoc PCC 7120. KS supervised the experimental work and was also involved in parts of the writing of the manuscript. PL conceived and coordinated the project and the manuscript. All authors have read and approved the manuscript.”
“Background In cyanobacteria there are Branched chain aminotransferase three enzymes directly involved in hydrogen metabolism; nitrogenase, uptake hydrogenase and bidirectional hydrogenase [1–3]. During nitrogen fixation, nitrogenase evolves molecular hydrogen (H2) as a by-product. The uptake hydrogenase consumes the H2 to recapture energy, thereby preventing losses from the cells, while the bidirectional hydrogenase has the capacity to both evolve and consume H2 [1–3]. The exact function of the bidirectional hydrogenase is unknown, but it has been proposed both to play a role in fermentation and to act as an electron valve during photosynthesis [2].