NDLI: [NiFe] Hydrogenase from Alteromonas macleodii with Unusual Stability in the Presence of Oxygen and High Temperature ▿ †

Content Provider	PubMed Central
Author	Vargas, Walter A. Weyman, Philip D. Tong, Yingkai Smith, Hamilton O. Xu, Qing
Copyright Year	2011
Abstract	Hydrogenases are enzymes involved in the bioproduction of hydrogen, a clean alternative energy source whose combustion generates water as the only end product. In this article we identified and characterized a [NiFe] hydrogenase from the marine bacterium Alteromonas macleodii “deep ecotype” with unusual stability toward oxygen and high temperature. The A. macleodii hydrogenase (HynSL) can catalyze both H2 evolution and H2 uptake reactions. HynSL was expressed in A. macleodii under aerobic conditions and reached the maximum activity when the cells entered the late exponential phase. The higher level of hydrogenase activity was accompanied by a greater abundance of the HynSL protein in the late-log or stationary phase. The addition of nickel to the growth medium significantly enhanced the hydrogenase activity. Ni treatment affected the level of the protein, but not the mRNA, indicating that the effect of Ni was exerted at the posttranscriptional level. Hydrogenase activity was distributed ∼30% in the membrane fraction and ∼70% in the cytoplasmic fraction. Thus, HynSL appears to be loosely membrane-bound. Partially purified A. macleodii hydrogenase demonstrated extraordinary stability. It retained 84% of its activity after exposure to 80°C for 2 h. After exposure to air for 45 days at 4°C, it retained nearly 100% of its activity when assayed under anaerobic conditions. Its catalytic activity in the presence of O2 was evaluated by the hydrogen-deuterium (H-D) exchange assay. In 1% O2, 20.4% of its H-D exchange activity was retained. The great stability of HynSL makes it a potential candidate for biotechnological applications.
Related Links	http://dx.doi.org/10.1128/AEM.01559-10
Starting Page	1990
File Format	PDF
ISSN	10985336
e-ISSN	10985336
Journal	Applied and Environmental Microbiology
Issue Number	6
Volume Number	77
Language	English
Publisher	American Society for Microbiology (ASM)
Publisher Date	2011-03-01
Access Restriction	Open
Rights Holder	American Society for Microbiology (ASM)
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Ecology Food Science Applied Microbiology and Biotechnology Biotechnology

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