The cyanobacterium Nostoc punctiforme ATCC 29133 (N. punctiforme) harbours two enzymes directly involved in production and consumption of molecular hydrogen: a nitrogenase and an uptake hydrogenase (Tamagnini

et al., 2002, 2007). The nitrogenase enzyme produces H2 as a byproduct during fixation of atmospheric N2 (Rees & Howard, 2000). Nitrogenases are oxygen sensitive, and in cyanobacteria of the genus Nostoc the enzyme is localized to heterocysts, specialized cells with a microaerobic environment due to the lack of O2-evolving activity of photosystem II, a high respiration rate, and a thick glycolipid envelope layer that reduces the flux of O2 (Flores & Herrero, 2010). The uptake hydrogenase catalyses the reoxidation of H2 formed by the nitrogenase, and thus recaptures GDC-0941 molecular weight the electrons from H2. The presence of the uptake hydrogenase is tightly connected to nitrogen fixation and all filamentous N2-fixing cyanobacteria contain an uptake hydrogenase (Ludwig et al., 2006). Upon deprivation of combined nitrogen, approximately every 10th–20th cell, evenly distributed in a filament of LY294002 in vitro Nostoc, differentiates into a heterocyst. During the heterocyst development, the transcription of the nif genes, encoding the nitrogenase, and the hup genes,

encoding the uptake hydrogenase, take place (Elhai & Wolk, 1990; Axelsson et al., 1999; Holmqvist, 2010). The uptake hydrogenase in cyanobacteria consists of a small (HupS) and a large (HupL) subunit, encoded by hupS and hupL, respectively. hupS and hupL are located in an operon, and transcribed as a single unit (Lindberg et al., 2000). The cellular

localization of the uptake hydrogenase in N2-fixing heterocyst-forming cyanobacteria is still not definite. Early work showed that in an aerobically grown culture of Nostoc PCC 7120, the activity of uptake hydrogenase is localized solely to the heterocysts (Peterson & Wolk, 1978; Houchins & Burris, 1981). This is in agreement with recent immunolocalization investigations where HupL was solely detected in the heterocysts of Nostoc PCC 7120 (Seabra et al., 2009). In Nostoc Rucaparib order PCC 7120, the expression of the hupSL is controlled by the removal of an excision element in hupL during heterocyst differentiation, which allows for a functional transcript only in the heterocyst (Carrasco et al., 1995, 2005). However, in N. punctiforme, no such rearrangement takes place (Oxelfelt et al., 1998) and immunolocalization studies have reported that HupL may be present in both heterocysts and vegetative cells (Lindblad & Sellstedt, 1990; Seabra et al., 2009). Nonetheless, as determined by investigation of the promoter activity of hupSL with a promoter-green fluorescent protein (GFP) construct, the transcription of hupSL takes place solely in the heterocysts (Holmqvist et al., 2009). The subcellular localization of the uptake hydrogenase is not fully resolved.