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Non-symbiotic hemoglobins (nsHbs) are widely distributed in land plants, including rice. These proteins are classified into type 1 (nsHbs-1) and type 2. The O  2 -affinity of nsHbs-1 is very high mostly because of an extremely low O  2 -dissociation rate constant resulting in that nsHbs-1 apparently do not release O  2  after oxygenation. Thus, it is possible that the  in   vivo  function of nsHbs-1 is other than O  2 -transport. Based on the properties of multiple Hbs it was proposed that nsHbs-1 could play diverse roles in rice organs, however the  in   vivo  activity of rice nsHbs-1 has been poorly analyzed. An  in   vivo  analysis for rice nsHbs-1 is essential to elucidate the biological function(s) of these proteins. Rice Hb1 and Hb2 are nsHbs-1 that have been generated in recombinant  E s  cherichia   coli  TB1. The rice Hb1 and Hb2 amino acid sequence, tertiary structure and rate and equilibrium constants for the reaction of O  2  are highly similar. Thus, it is possible that rice Hb1 and Hb2 function similarly  in   vivo . As an initial approach to test this hypothesis we analyzed the effect of the synthesis of rice Hb1 and Hb2 in the recombinant  E .  coli  TB1 growth. Effect of the synthesis of the O  2 -carrying soybean leghemoglobin  a , cowpea leghemoglobin II and  Vitreoscilla  Hb in the recombinant  E .  coli  TB1 growth was also analyzed as an O  2 -carrier control. Our results showed that synthesis of rice Hb1, rice Hb2, soybean Lb  a , cowpea LbII and  Vitreoscilla  Hb inhibits the recombinant  E .  coli  TB1 growth and that growth inhibition was stronger when recombinant  E .  coli  TB1 synthesized rice Hb2 than when synthesized rice Hb1. These results suggested that rice Hb1 and Hb2 could function differently  in vivo .

Effect of the synthesis of rice non-symbiotic hemoglobins 1 and 2 in the recombinant Escherichia coli TB1 growth