Advances in[Fe]-hydrogenase from methanogens

Abstract:

Hydrogenases are classified into tree types including[NiFe]-,[FeFe]- and[Fe]-hydrogenase depending on the different metals in the active center.[NiFe]- and[FeFe]-hydrogenases were found in various bacteria, while[Fe]-hydrogenase was only found in hydrogenotrophic methanogens. It catalyzes the hetero cleavage of H₂ to reduce the methenyl group of C1 carrier tetrahydrobiopterin into methylene group. Different from other two types of hydrogenases,[Fe]-hydrogenases do not contain electron-transmitting iron-sulfur clusters and bimetallic active centers. Additionally, the highly substituted pyridine ring and the Fe-acyl carbon bond in active center of[Fe]-hydrogenase indicated that there might be a new catalytic mechanism in hydrogenase. It also proposed that methanogens could synthesis this unique structural cofactor in a special way. This review summarizes the research progress of[Fe]-hydrogenase since its discovery in 1990, including physiological function, structural characteristics, catalytic mechanism, maturation process, and industrial application in future.

Key words:hydrogenase;methanogens;protein structure;catalytic mechanism;biosynthetic pathway