The role of hydrogen metabolism in photoheterotrophic cultures of the cyanobacterium Nostoc sp. strain Cc isolated from Cycas circinalis L.

Tredici, Mario R.; Margheri, M. C.; Philippis, Roberto De; Materassi, R.

doi:10.1099/00221287-136-6-1009

Cited by 10 publications

(5 citation statements)

References 23 publications

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“…This finding is in agreement with the suggested coupling between hydrogen consumption and an efficient nitrogen fixation in Nostoc sp. strain Cc and other symbiotic microorganisms (122,124,202). In contrast, autotrophically grown cells of a cyanobacterium isolated from Macrozamia communis have a higher level of both nitrogenase and hydrogenase activity than do heterotrophically grown cells (46).…”

Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

“…Cyanobacterial hydrogenases seem to be no exception. In several strains the hydrogen uptake activity is dependent on the concentration of nickel in the growth medium (45,46,151,152,182,202,224).…”

Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

“…However, recent data clearly demonstrated that, at least in nitrogen-fixing strains, it is not an universal enzyme and that strains missing the bidirectional enzyme have nothing obvious in common (192,194). The Ni-containing bidirectional hydrogenase, partially purified and characterized from A. variabilis ATCC 29413 (178) differs from the uptake hydrogenase in its physical and catalytic properties (178,202). In general, cyanobacterial bidirectional hydrogenases are characterized by their sensitivity to oxygen, thermotolerance, and high affinity to hydrogen (49,87,89,163,178).…”

Section: Cyanobacterial Bidirectional Hydrogenasesmentioning

confidence: 99%

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Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

464

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 Uptake Hydrogenasesmentioning

confidence: 99%

Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

Section: Cyanobacterial Bidirectional Hydrogenasesmentioning

confidence: 99%

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Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

464

372

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“…Cyanobacteria may possess several enzymes involved in hydrogen metabolism: (i) a nitrogenase, catalyzing the production of H 2 concomitantly with the reduction of N 2 to NH 3 (7,11,32); (ii) an uptake hydrogenase, catalyzing the consumption of H 2 produced by the nitrogenase (15,17,21,33); and (iii) a bidirectional hydrogenase, which has the capacity to both take up and produce H 2 (8-10, 16, 23, 26, 28, 29) (for a general review, see reference 30).…”

mentioning

confidence: 99%

Hydrogenases in Nostoc sp. Strain PCC 73102, a Strain Lacking a Bidirectional Enzyme

Tamagnini¹,

Troshina²,

Oxelfelt³

et al. 1997

Appl Environ Microbiol

109

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The present study was carried out in order to examine and characterize the bidirectional hydrogenase in the cyanobacterium Nostoc sp. strain PCC 73102. Southern hybridizations with the probes Av1 and Av3 (hoxY and hoxH, bidirectional hydrogenase small and large subunits, respectively) revealed the occurrence of corresponding sequences in Anabaena variabilis (control), Anabaena sp. strain PCC 7120, and Nostoc muscorum but not in Nostoc sp. strain PCC 73102. As a control, hybridizations with the probe hup2 (hupL, uptake hydrogenase large subunit) demonstrated the presence of a corresponding gene in all the cyanobacteria tested, including Nostoc sp. strain PCC 73102. Moreover, with three different growth media, a bidirectional enzyme that was functional in vivo was observed in N. muscorum, Anabaena sp. strain PCC 7120, and A. variabilis, whereas Nostoc sp. strain PCC 73102 consistently lacked any detectable in vivo activity. Similar results were obtained when assaying for the presence of an enzyme that is functional in vitro. Native polyacrylamide gel electrophoresis followed by in situ hydrogenase activity staining was used to demonstrate the presence or absence of a functional enzyme. Again, bands corresponding to hydrogenase activity were observed for N. muscorum, Anabaena sp. strain PCC 7120, and A. variabilis but not for Nostoc sp. strain PCC 73102. In conclusion, we were unable to detect a bidirectional hydrogenase in Nostoc sp. strain PCC 73102 with specific physiological and molecular techniques. The same techniques clearly showed the presence of an inducible bidirectional enzyme and corresponding structural genes in N. muscorum, Anabaena sp. strain PCC 7120, and A. variabilis. Hence, Nostoc sp. strain PCC 73102 seems to be an unusual cyanobacterium and an interesting candidate for future biotechnological applications.

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“…strain Cc or non-N 2 -fixing cyanobacterium Synechocystis sp. PCC 6803, both of which were able to utilize glucose for hydrogen production [18,25]. Hydrogen production decreased with glucose concentrations higher than 0.2% (Fig.…”

Section: 2mentioning

confidence: 96%