TAILIEUCHUNG - Báo cáo khoa học: A kinetic approach to the dependence of dissimilatory metal reduction by Shewanella oneidensis MR-1 on the outer membrane cytochromes c OmcA and OmcB

The Gram-negative bacterium Shewanella oneidensis MR-1 shows a remarkably versatile anaerobic respiratory metabolism. One of its hall-marks is its ability to grow and survive through the reduction of metallic compounds. Among other proteins, outer membrane decaheme cyto-chromesc OmcA and OmcB have been identified as key players in metal reduction. | ễFEBS Journal A kinetic approach to the dependence of dissimilatory metal reduction by Shewanella oneidensis MR-1 on the outer membrane cytochromes c OmcA and OmcB Jimmy Borloo Bjorn Vergauwen Lina De Smet Ann Brige Bart Motte Bart Devreese and Jozef Van Beeumen Laboratory for Protein Biochemistry and Protein Engineering Ghent University Belgium Keywords kinetic enzyme parameters metal reduction outer membrane cytochromes c OmcA and OmcB Shewanella oneidensis MR-1 terminal reductases Correspondence J. Borloo Laboratory for Protein Biochemistry and Protein Engineering Ghent University . Ledeganckstraat 35 B-9000 Ghent Belgium Fax 32 9 264 52 73 Tel 32 9 264 51 26 E-mail Website http . be These authors contributed equally to this work Received 28 April2007 revised 25 May 2007 accepted 30 May 2007 doi The Gram-negative bacterium Shewanella oneidensis MR-1 shows a remarkably versatile anaerobic respiratory metabolism. One of its hallmarks is its ability to grow and survive through the reduction of metallic compounds. Among other proteins outer membrane decaheme cytochromes c OmcA and OmcB have been identified as key players in metal reduction. In fact both of these cytochromes have been proposed to be terminal Fe III and Mn IV reductases although their role in the reduction of other metals is less well understood. To obtain more insight into this we constructed and analyzed omcA omcB and omcA omcB insertion mutants of S. oneidensis MR-1. Anaerobic growth on Fe III V V Se VI and U VI revealed a requirement for both OmcA and OmcB in Fe III reduction a redundant function in V V reduction and no apparent involvement in Se VI and U VI reduction. Growth of the omcB mutant on Fe III was more affected than growth of the omcA mutant suggesting OmcB to be the principal Fe III reductase. This result was corroborated through the examination of whole cell kinetics of OmcA- and .

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