Isolation and characterization of the hydrogenase activity from the non‐heterocystous cyanobacterium <i>Spirulina maxima</i>

Llama, Marı́a J.; Serra, Juan L.; Rao, K. K.; Hall, D.O.

doi:10.1016/0014-5793(79)80213-6

Cited by 48 publications

(12 citation statements)

References 22 publications

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“…As with the uptake hydrogenase, molecular studies helped to clarify the picture of the subunit composition and molecular mass of the bidirectional hydrogenase. In agreement with the molecular data, previous work referred to large subunits of about 50 to 56 kDa in A. variabilis, Synechococcus strain PCC 6301, M. aeruginosa, and Spirulina plantensis (15,96,118) and to small subunits of about 17 kDa in A. variabilis and Synechococcus strain PCC 6301 (96). In A. variabilis, hoxH and hoxY encode predicted polypeptides of 54.8 and 22.5 kDa, respectively (173).…”

Section: Cyanobacterial Bidirectional Hydrogenasessupporting

confidence: 83%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

466

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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Section: Cyanobacterial Bidirectional Hydrogenasessupporting

confidence: 83%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

466

372

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“…claims in the literature [35,36] that cyanobacterial hydrogenases are dam aged by oxygen, but the oppo site has also been reported [14,19]. This aspect has not been studied systematically in the present investi gation.…”

Section: W Henmentioning

confidence: 62%

“…This aspect has not been studied systematically in the present investi gation. The 0 2-sensitivity of the hydrogenase may differ with the oxidation state of the enzyme, and the oxidation state of the enzyme may change within the isolation protocol [3,35]. Therefore all purification steps were routinely perform ed under argon.…”

Section: W Henmentioning

confidence: 99%

Localization of the Reversible Hydrogenase in Cyanobacteria

Kentemich

Bahnweg

Mayer

et al. 1989

Zeitschrift Für Naturforschung C

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“…However their molecular properties are not well characterized. A hydrogenase preparation from Spirulina maxima was reported to be a monomer of 56 kDa [12], while one from Anabaena cylindrica consisted of two nonidentical subunits of 42 and 50 kDa [13]. The reversible hydrogenases from Anacystis nidulans and A. variabilis have been reported to have dimeric structures [14,15].…”

Section: Introductionmentioning

confidence: 99%