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[FeFe]-Hydrogenase: Catalytic Center and Modification by Genetic Engineering

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Advances in Applied Biotechnology

Part of the book series: Lecture Notes in Electrical Engineering ((LNEE,volume 333))

Abstract

In this review, we highlight the [FeFe]-hydrogenase, which is capable of catalyzing the splitting of molecular hydrogen to produce electrons and protons or catalyzing the reversible reaction: 2H+ + 2e− = H2↑ as a potential renewable fuel. We have focused on [FeFe]-hydrogenase because of structural studies have shed more light on the hydrogenase activity than the [NiFe]-hydrogenase. Our studies on the [FeFe]-hydrogenase from Chlamydomonas reinhardtii CC-503 (HydA 1) have also been highlighted. There are two factors influencing the multiplexed hydrogenase activity: a single hydrophobic channel of catalytic center, which is known as the H-cluster active site based on site-directed mutagenesis, moreover, some promising results have already been obtained. Modifications of [FeFe]-hydrogenase can improve its stabilization and activity in vitro, increase the efficiency of bioenergy utilization, and promote industrial amplification of biofuel production.

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Authors and Affiliations

  1. China University of Petroleum (East China), No. 66, Chang Jiang West Road, Economic & Technological Development Zone, Qingdao, 266580, People’s Republic of China

    Jiayi He & Chunfei Wu

Authors
  1. Jiayi He
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  2. Chunfei Wu
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Correspondence to Jiayi He .

Editor information

Editors and Affiliations

  1. Tianjin University of Science and Technology, Tianjin, China

    Tong-Cun Zhang

  2. SBI ALApromo, Tokyo, Japan

    Motowo Nakajima

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He, J., Wu, C. (2015). [FeFe]-Hydrogenase: Catalytic Center and Modification by Genetic Engineering. In: Zhang, TC., Nakajima, M. (eds) Advances in Applied Biotechnology. Lecture Notes in Electrical Engineering, vol 333. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-46318-5_64

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