Activation of formate hydrogen-lyase via expression of uptake [NiFe]-hydrogenase in Escherichia coli BL21(DE3)

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Activation of formate hydrogen-lyase via expression of uptake [NiFe]-hydrogenase in Escherichia coli BL21(DE3)

BACKGROUND Several recent studies have reported successful hydrogen (H2) production achieved via recombinant expression of uptake [NiFe]-hydrogenases from Hydrogenovibrio marinus, Rhodobacter sphaeroides, and Escherichia coli (hydrogenase-1) in E. coli BL21(DE3), a strain that lacks H2-evolving activity. However, there are some unclear points that do not support the conclusion that the recombin...

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Enhanced hydrogen production from formic acid by formate hydrogen lyase-overexpressing Escherichia coli strains.

Genetic recombination of Escherichia coli in conjunction with process manipulation was employed to elevate the efficiency of hydrogen production in the resultant strain SR13 2 orders of magnitude above that of conventional methods. The formate hydrogen lyase (FHL)-overexpressing strain SR13 was constructed by combining FHL repressor (hycA) inactivation with FHL activator (fhlA) overexpression. ...

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Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in Escherichia coli

BACKGROUND Hydrogenases catalyze reversible reaction between hydrogen (H2) and proton. Inactivation of hydrogenase by exposure to oxygen is a critical limitation in biohydrogen production since strict anaerobic conditions are required. While [FeFe]-hydrogenases are irreversibly inactivated by oxygen, it was known that [NiFe]-hydrogenases are generally more tolerant to oxygen. The physiological ...

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Carbon metabolism regulates expression of the pfl (pyruvate formate-lyase) gene in Escherichia coli.

The anaerobic expression of pfl is reduced both in a strain mutated in the pgi gene and in a pfkA pfkB double mutant strain when cells are grown in medium supplemented with glucose. When cells are grown in medium supplemented with either fructose or pyruvate, no reduction is observed in these strains. The amount of pyruvate in the cells may be responsible for the reduced expression of pfl in th...

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Pyruvate Formate-Lyase Enables Efficient Growth of Escherichia coli on Acetate and Formate.

Pyruvate formate-lyase (PFL) is a ubiquitous enzyme that supports increased ATP yield during sugar fermentation. While the PFL reaction is known to be reversible in vitro, the ability of PFL to support microbial growth by condensing acetyl-CoA and formate in vivo has never been directly tested. Here, we employ Escherichia coli mutant strains that cannot assimilate acetate via the glyoxylate shu...

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ژورنال

عنوان ژورنال: Microbial Cell Factories

سال: 2015

ISSN: 1475-2859

DOI: 10.1186/s12934-015-0343-0