Hydrogenase: a bacterial enzyme activating molecular hydrogen

“…The capacity of certain microorganisms to metabolize molecular hydrogen was discovered at the end of the 19th century (85) and later identified to be catalyzed by a hydrogenase (191). Since then hydrogenases have been observed and characterized in many microorganisms, including some algae, trichomonads, anaerobic ciliates, and chytrid fungi (4,5,59,77,86,94,100,176,222,223,225).…”

Section: Hydrogenasesmentioning

confidence: 99%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

462

372

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Cyanobacteria may possess several enzymes that are directly involved in dihydrogen metabolism: nitrogenase(s) catalyzing the production of hydrogen concomitantly with the reduction of dinitrogen to ammonia, an uptake hydrogenase (encoded by hupSL) catalyzing the consumption of hydrogen produced by the nitrogenase, and a bidirectional hydrogenase (encoded by hoxFUYH) which has the capacity to both take up and produce hydrogen. This review summarizes our knowledge about cyanobacterial hydrogenases, focusing on recent progress since the first molecular information was published in 1995. It presents the molecular knowledge about cyanobacterial hupSL and hoxFUYH, their corresponding gene products, and their accessory genes before finishing with an applied aspect—the use of cyanobacteria in a biological, renewable production of the future energy carrier molecular hydrogen. In addition to scientific publications, information from three cyanobacterial genomes, the unicellular Synechocystis strain PCC 6803 and the filamentous heterocystous Anabaena strain PCC 7120 and Nostoc punctiforme (PCC 73102/ATCC 29133) is included

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“…The work of my group on the biochemistry of methanogenesis started with growth experiments and the discovery that growth of methanogens is dependent on nickel (Schonheit et al, 1979). This led to the finding that coenzyme F430 is a nickel porphinoid (Diekert et al, 1980a, b), that carbon monoxide dehydrogenase from methanogens contains nickel (Hammel et al, 1984) and that the hydrogenases first described by Marjory Stephenson (Stephenson & Stickland, 1931a) are nickel enzymes (Graf & Thauer, 1981;Albracht et al, 1982;Albracht, 1994) (for recent reviews on nickel enzymes including methyl-coenzyme M reductase see Cammack & van Vliet, 1998;Maroney et al, 1998). Later we found that methanogens also contain a metal-free hydrogenase (Zirngibl et al, 1990;Thauer et al, 1996) and just recently that methanogens contain a fourth type of hydrogenase (Kiinkel et al, 1998) that shows sequence similarity to hydrogenase 3 (Sauter et al, 1992) and 4 (Andrews et al, 1997) of the formate hydrogenlyase from E. coli, an enzyme complex first studied in detail in the laboratory of Marjory Stephenson now almost 70 years ago (Stickland, 1929 ; Stephenson & Stickland, 1932& Stickland, ,1933bWoods, 1936).…”

Section: From Hydrogenase To Methyl-coenzyme M Reductasementioning

confidence: 99%

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

1998

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Historical overview In 1933, Stephenson & Stickland (1933a) published that they had isolated from river mud, by the single cell technique, a methanogenic organism capable of growth in an inorganic medium with formate as the sole carbon source. 4 H C 0 0-+ 4H' + CH, + 3 C 0 , + 2H,O AGO' =-144-5 kJ mol-' Methane formation from formate was shown to occur in a stepwise manner, by the preliminary decomposition of formic acid into CO, and H, followed by a reduction of CO, by H,, suggesting that formate was not an intermediate in the reduction of CO, to methane. HCOO-+ H+-+ H, + CO, 4H,+CO,-+ C H , + 2 H 2 0 AGO' =-3-5 kJ mol-' AGO' =-131 kJ mol-' Cell suspensions of the microorganism catalysed the reduction of methylene blue with H,, indicating that the methanogen contained an enzyme which activates molecular hydrogen. H,-+ 2e-+ 2H+ E; =-414mV This enzyme had been discovered by Stephenson & Stickland (1931a) 2 years before in a number of bacterial species and was named by them 'hydrogenase'. The paper by Stephenson & Stickland (1933a) is considered to mark the beginning of the modern era for study of methanogenesis (Wolfe, 1993). It is the first Except when otherwise noted, the free energy changes given for methanogenic reactions were calculated from the free energies of formation from the elements of the substrates and products with non-gaseous compounds at 1 M aqueous solution and gaseous compounds in the gaseous state at 1 atmosphere pressure (101 kPa). The free energy changes of formation were taken from Thauer eta/. (1977). 0002-2667 0 1998 SGM Glucose-+ 3C0, + 3CH, AGO' =-418.1 kJ mol-' This reaction is not catalysed by single microorganisms but by syntrophic associations of microorganisms. First the glucose is fermented to acetate, CO, and H, or to acetate, formate and H, : Glucose + 2H,O + 2CH3COO-+ 2H' + 2C0, + 4H2 AGO' =-215.7 kJ mol-' Glucose + 2H20-+ 2CH3COO-+ 2HC00-+ 4H' + 2H, AGO' =-208.7 kJ mol-1 These fermentations are brought about by strictly anaerobic bacteria and/or protozoa. In a second step, the products of glucose fermentation are then converted to methane, the rate of conversion being such that the concentrations of acetate (< 1 mM), formate (< 0.1 mM) and H, (< 1 pM) in the anaerobic sediments remain very low (Zinder, 1993). CH3COO-+Hf-+ C02+CH, AGO' =-36 kJ mol-' 4H, + CO,-+ CH, + 2H20 AGO' =-131 kJ mol-' 4HC00-+4H+ + CH,+3C02+2H,0 AGO' =-144.5 kJ mol-' H-S-CoM, coenzyme M ; H-S-COB, coenzyme B ; H,SPT, tetrahydrosarcinapterin, which is the modified tetrahydromethanopterin (for structures see Fig. 3) present in the Methanosarcinales (Gorris & van der Drift, 1994). Reaction" Enzyme (gene) Most recent literature Acetate + CoA + acetyl-CoA + H,O AGO' = + 35.7 k J rnol-lt

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Hydrogenase: a bacterial enzyme activating molecular hydrogen

Cited by 316 publications

References 3 publications

A positive role for hydrogen gas in adventitious root development

A positive role for hydrogen gas in adventitious root development

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

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