Thermotolerant hydrogenases: biological diversity, properties, and biotechnological applications.
Hydrogenases are metalloproteins that catalyze the oxidation and reduction of molecular hydrogen and play a crucial role in many microbial metabolic processes. A subset of hydrogenases capable of functioning at temperatures from 50 to 125 degrees C is found in thermophilic microorganisms. Most known thermotolerant hydrogenases contain a [NiFe] active site and are either bidirectional or uptake type. Although no exhaustive survey has been done of the ecological diversity of thermophilic hydrogen-reducing or oxidizing bacteria, they appear to exist in virtually every thermophilic environment examined to date. Thermotolerant hydrogenases share many similarities with their mesophilic counterparts, but they have several features in addition to thermotolerance that make them especially well suited for biotechnological applications. Ongoing research is focused on potential applications of thermotolerant H2 ases in biosynthesis, H2 production, bioremediation, and biosensors.
Eberly
Jed O
JO
Department of Biological & Ecological Engineering, Oregon State University, Corvallis, Oregon 97331, USA.
Ely
Roger L
RL
D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D004795:Enzyme Stability; D006358:Hot Temperature; D006864:Hydrogenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D006864:Hydrogenase