Escherichia coli hydrogenase 3 is a reversible enzyme possessing hydrogen uptake and synthesis activities

2007 ◽  
Vol 76 (5) ◽  
pp. 1035-1042 ◽  
Author(s):  
Toshinari Maeda ◽  
Viviana Sanchez-Torres ◽  
Thomas K. Wood
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Uptake ◽  
Hydrogenase 3

scholarly journals Molecular Hydrogen Formation by Escherichia Coli Hydrogenase 3 during Fermentation of Glucose at Slightly Acidic pH

2011 ◽  
Vol 100 (3) ◽  
pp. 488a
Author(s):  
Anna Poladyan ◽  
Anna Poghosyan ◽  
Karen Trchounian ◽  
Armen Trchounian
Keyword(s):  
Escherichia Coli ◽  
Molecular Hydrogen ◽  
Acidic Ph ◽  
Hydrogen Formation ◽  
Hydrogenase 3

Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli

1999 ◽  
Vol 173 (2) ◽  
pp. 110-116 ◽  
Author(s):  
Ekaterini Theodoratou ◽  
Athanasios Paschos ◽  
Susan Mintz-Weber ◽  
August Böck
Keyword(s):  
Escherichia Coli ◽  
Cleavage Site ◽  
Large Subunit ◽  
Site Specificity ◽  
Hydrogenase 3

scholarly journals Interplay between the Specific Chaperone-Like Proteins HybG and HypC in Maturation of Hydrogenases 1, 2, and 3 from Escherichia coli

2001 ◽  
Vol 183 (9) ◽  
pp. 2817-2822 ◽  
Author(s):  
Melanie Blokesch ◽  
Axel Magalon ◽  
August Böck
Keyword(s):  
Escherichia Coli ◽  
Complex Formation ◽  
Gene Product ◽  
Genetic Background ◽  
Large Subunit ◽  
Cysteine Residue ◽  
Maturation Process ◽  
Hydrogenase 3 ◽  
Hydrogenase 2

ABSTRACT The hybG gene product from Escherichia colihas been identified as a chaperone-like protein acting in the maturation of hydrogenases 1 and 2. It was shown that HybG forms a complex with the precursor of the large subunit of hydrogenase 2. As with HypC, which is the chaperone-like protein involved in hydrogenase 3 maturation, the N-terminal cysteine residue is crucial for complex formation. Introduction of a deletion into hybG abolished the generation of active hydrogenase 2 but only quantitatively reduced hydrogenase 1 activity since HypC could replace HybG in this function. In contrast, HybG could not take over the role of HypC in a ΔhypC genetic background. Overproduction of HybG, especially of the variants with the replaced N-terminal cysteine residue, strongly interfered with hydrogenase 3 maturation, apparently by titrating some other component(s) of the maturation machinery. The results indicate that the three hydrogenase isoenzymes not only are interacting at the functional level but are also interconnected during the maturation process.

scholarly journals Network of Hydrogenase Maturation in Escherichia coli: Role of Accessory Proteins HypA and HybF

2002 ◽  
Vol 184 (14) ◽  
pp. 3879-3885 ◽  
Author(s):  
Michaela Hube ◽  
Melanie Blokesch ◽  
August Böck
Keyword(s):  
Escherichia Coli ◽  
Double Mutant ◽  
Residual Activity ◽  
Accessory Proteins ◽  
Hydrogenase Maturation ◽  
Residual Level ◽  
High Nickel ◽  
Hydrogenase 3 ◽  
Minimal Residual

ABSTRACT We have studied the roles of the auxiliary protein HypA and of its homolog HybF in hydrogenase maturation. A mutation in hypA leads to the nearly complete blockade of maturation solely of hydrogenase 3 whereas a lesion in hybF drastically but not totally reduces maturation and activity of isoenzymes 1 and 2. The residual level of matured enzymes in the hybF mutant was shown to be due to the function of HypA; HybF, conversely, was responsible for a minimal residual activity of hydrogenase 3 in the mutant hypA strain. Accordingly, a hypA ΔhybF double mutant was completely blocked in the maturation process. However, the inclusion of high nickel concentrations in the medium could restore limited activity of all three hydrogenases. The results of this study and of previous work (M. Blokesch, A. Magalon, and A. Böck, J. Bacteriol. 189:2817-2822, 2001) show that the maturation of the three functional hydrogenases from Escherichia coli is intimately connected via the activity of proteins HypA and HypC and of their homologs HybF and HybG, respectively. The results also support the suggestion of Olson et al. (J. W. Olson, N. S. Mehta, and R. J. Maier, Mol. Microbiol. 39:176-182, 2001) that HypA cooperates with HypB in the insertion of nickel into the precursor of the large hydrogenase subunit. Whereas HypA is predominantly involved in the maturation of hydrogenase 3, HybF takes over its function in the maturation of isoenzymes 1 and 2.

scholarly journals An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea

1998 ◽  
Vol 252 (3) ◽  
pp. 467-476 ◽  
Author(s):  
Andreas Kunkel ◽  
Julia A. Vorholt ◽  
Rudolf K. Thauer ◽  
Reiner Hedderich
Keyword(s):  
Escherichia Coli ◽  
Methanogenic Archaea ◽  
Hydrogenase 3

scholarly journals Expression and Regulation of a Silent Operon, hyf, Coding for Hydrogenase 4 Isoenzyme in Escherichia coli

2004 ◽  
Vol 186 (2) ◽  
pp. 580-587 ◽  
Author(s):  
William T. Self ◽  
Adnan Hasona ◽  
K. T. Shanmugam
Keyword(s):  
Escherichia Coli ◽  
Cyclic Amp ◽  
Type Strain ◽  
Wild Type Strain ◽  
Receptor Protein ◽  
Wild Type ◽  
Anaerobic Conditions ◽  
Heterologous Promoter ◽  
Cyclic Amp Receptor Protein ◽  
Hydrogenase 3

ABSTRACT On the basis of hyf-lacZ fusion studies, the hyf operon of Escherichia coli, noted for encoding the fourth hydrogenase isoenzyme (HYD4), is not expressed at a significant level in a wild-type strain. However, mutant FhlA proteins (constitutive activators of the hyc-encoded hydrogenase 3 isoenzyme) activated hyf-lacZ. HyfR, an FhlA homolog encoded by the hyfR gene present at the end of the hyf operon, also activated transcription of hyf-lacZ but did so only when hyfR was expressed from a heterologous promoter. The HYD4 isoenzyme did not substitute for HYD3 in H2 production. Optimum expression of hyf-lacZ required the presence of cyclic AMP receptor protein-cyclic AMP complex and anaerobic conditions when HyfR was the activator.

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