TAILIEUCHUNG - Báo cáo khoa hoc : Role of HoxE subunit in Synechocystis PCC6803 hydrogenase

Cyanobacterial NAD(P) + -reducing reversible hydrogenases comprise five subunits. Four of them (HoxF, HoxU, HoxY, and HoxH) are also found in the well-described related enzyme from Ralstonia eutropha. | IFEBS Journal Role of HoxE subunit in Synechocystis PCC6803 hydrogenase Emeline Aubert-Jousset1 2 3 Melissa Cano1 2 3 Genevieve Guedeney1 2 3 Pierre Richaud1 2 3 and Laurent Cournac1 2 3 1 CEA DSV IBEB Laboratoire de Bioénergétique et Biotechnologie des Bacteries Microalgues Saint PaulLez Durance France 2 CNRS UMR Biologie Vegetale Microbiologie Environnementales Saint Paullez Durance France 3 Aix-Marseille Universite Saint Paullez Durance France Keywords activation cyanobacteria diaphorase Hox genes hydrogen Correspondence L. Cournac CEA Cadarache IBEB Bat 161 13108 Saint PaulLez Durance France Fax 33 4 42 25 62 65 Tel 33 4 42 25 43 66 E-mail Received 8 March 2011 revised 10 August 2011 accepted 12 August 2011 doi Cyanobacterial NAD P -reducing reversible hydrogenases comprise five subunits. Four of them HoxF HoxU HoxY and HoxH are also found in the well-described related enzyme from Ralstonia eutropha. The fifth one HoxE is not encoded in the R. eutropha genome but shares homology with the N-terminal part of R. eutropha HoxF. However in cyanobacteria HoxE contains a 2Fe-2S cluster-binding motif that is not found in the related R. eutropha sequence. In order to obtain some insights into the role of HoxE in cyanobacteria we deleted this subunit in Synechocys-tis PCC6803. Three types of interaction of the cyanobacterial hydrogenase with pyridine nucleotides were tested a reductive activation of the NiFe site for which NADPH was found to be more efficient than NADH b H2 production for which NADH appeared to be a more efficient electron donor than NADPH and c H2 oxidation for which NAD was a much better electron acceptor than NADP . Upon hoxE deletion the Synecho-cystis hydrogenase active site remained functional with artificial electron donors or acceptors but the enzyme became unable to catalyze H2 production or uptake with NAD NAD . However activation of the electron transfer-independent H D exchange reaction

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